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Department of Biochemistry, Rollins Research Center, Emory University, Atlanta, GA 30322-3050
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ABSTRACT |
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 TOP ABSTRACT INTRODUCTIONVitamin B-6 metabolismFlavin metabolismFlavocoenzyme functionBiotin metabolismLipoate metabolismTransport and uptake of...Metal ionsOtherREFERENCES |
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KEY WORDS: • cofactors • water-soluble vitamins • coenzymes • divalent cations • vitamin metabolism
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INTRODUCTION |
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TOPABSTRACTINTRODUCTIONVitamin B-6 metabolismFlavin metabolismFlavocoenzyme functionBiotin metabolismLipoate metabolismTransport and uptake of...Metal ionsOtherREFERENCES |
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My doctoral dissertation research, mentored by Professor Oscar Touster
at Vanderbilt, was on pentose and pentitol metabolism. Studies on
isotopically labeled pentitols and pentoses helped establish the
metabolic interrelationships of xylitol/xylulose to glucose/glucuronate
(Touster et al. 1957
) and further to the pentose
phosphate pathway (McCormick and Touster 1957
). The
general interdigitations of pentitol metabolism were extended
(McCormick and Touster 1961
) and the genetic defect of
essential pentosuria clarified. Because one extension of glucuronate
metabolism is toward ascorbate (vitamin C) as well as xylulose, and
there was a strong interest in nutritional biochemistry within the
Vanderbilt department when Bill Darby was chairman, my polarized
interests were to head west where there were strong elements of
vitamin/coenzyme research at the University of California-Berkeley.
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Vitamin B-6 metabolism |
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TOPABSTRACTINTRODUCTIONVitamin B-6 metabolismFlavin metabolismFlavocoenzyme functionBiotin metabolismLipoate metabolismTransport and uptake of...Metal ionsOtherREFERENCES |
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During postdoctoral research with Professor Esmond Snell at Berkeley, I
began work initiated by M. Gregory. Isolation and comparative studies
on both pro- and eucaryotic forms of pyridoxal kinase delineated
general properties, including the first substantiated role of
Zn2+ in preference to Mg2+ as the cosubstrate
ATP complex for the mammalian phosphokinase (McCormick et al. 1961
), and led to circumscription of inhibitory aspects
(McCormick and Snell 1961
), including the potent action
of carbonyl reagents (McCormick 1959
, McCormick et al. 1960
, McCormick and Snell 1959
) and such
drugs as are known to bind to the kinase (McCormick and Chen 1999
).
Pyridoxine (pyridoxamine) 5'-phosphate oxidase—P. Barsa, D. Bowers-Komro, H. Chen, J. Choi, M. Davis, M. DePecol, D. Edmondson, K. Horiike, S. Kasai, M. Kazarinoff, W. Korytnyk, K. Matsui, A. Merrill, K. Ohashi, K. Rasmussen, D. Roe, H. Tsuge, K. Watanabe.
As a faculty member at Cornell and Emory with the help of graduate and
postdoctoral coworkers, we succeeded in the first complete purification
of pyridoxine (pyridoxamine) 5'-phosphate oxidase, the flavin
mononucleotide (FMN)2
-dependent enzyme responsible for
conversion of the kinase-derived phosphovitamin B-6 to coenzymic
pyridoxal 5'-phosphate (Kazarinoff and McCormick 1975
).
More facile affinity purifications (Bowers-Komro et al. 1986
, Tsuge and McCormick 1980
) and assays
(DePecol and McCormick 1980
) were developed and
circumscription of substrate (DePecol and McCormick 1980
, Bowers-Komro and McCormick 1987
,
Kazarinoff and McCormick 1973
, Kazarinoff and McCormick 1975
, Merrill et al. 1980
) and
coenzyme specificities (Kazarinoff and McCormick 1974
,
Merrill et al. 1979b
) accomplished. Systematic
elucidation of the dimeric subunit association (Horiike et al. 1979a
, Tsuge and McCormick 1980
),
active-site amino acid residues (Bowers-Komro et al. 1986
, Choi and McCormick 1981
, Horiike et al. 1979b
, McCormick et al. 1976
, Tsuge and McCormick 1980
), kinetics (Choi et al. 1982
,
Choi et al. 1983
), and ultimately mechanistic
delineation of stereochemical aspects (Bowers-Komro and McCormick 1984b
, Bowers-Komro and McCormick 1985a
, McCormick and Bowers-Komro 1986
) have
provided definitive information on the way this essential flavoprotein
operates (Bowers-Komro and McCormick 1984a
), depends
upon flavin status of an organism (Rasmussen et al. 1979
, Rasmussen et al. 1980
), and participates
in the regulation of B-6 metabolism (McCormick and Merrill 1980
, Merrill et al. 1978b
). The sequences for
this essential oxidase from several organisms have been determined
(McCormick and Chen 1999
). An important interface
between vitamins B-2 and B-6 is now clear.
The scheme given in Figure 1
outlines the sequential roles of kinase and oxidase in the
interconversions of B-6 vitamers toward the coenzyme pyridoxal 5'
phosphate.
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Flavin metabolism |
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TOPABSTRACTINTRODUCTIONVitamin B-6 metabolismFlavin metabolismFlavocoenzyme functionBiotin metabolismLipoate metabolismTransport and uptake of...Metal ionsOtherREFERENCES |
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The first significant purification of flavokinase, shown by us to be
another Zn2+ preferring enzyme (McCormick 1962
, Merrill and McCormick 1980
, Nakano and McCormick 1991b
) responsible for catalyzing phosphorylation
of riboflavin to yield FMN, was accomplished with classic techniques
(McCormick 1962
) and completely purified from mammalian
tissues by "affinity techniques" (Arsenis and McCormick 1964a
, Merrill and McCormick 1980
, Nakano and McCormick 1991a
) before the term and practice became
commonplace. Detailed studies on the specificity of this enzyme
(Chassy et al. 1965
, McCormick and Butler 1962
, McCormick et al. 1963
, McCormick et al. 1964,
Yang et al. 1964
) helped clarify the
biological activities of flavin analogs. Investigations of substrate
induction (Lee and McCormick 1983
, Merrill et al. 1978a
) and thyroid hormone stimulation (Lee and McCormick 1985
, McCormick et al. 1984
) have led
to recognition of the "active" and "inactive" forms which are
poised at the regulation site of flavocoenzyme biosynthesis.
FAD synthetase—D. Bowers-Komro, B. Gomes, H. Hartmann, S. Lee, A. Merrill, H. Nakano, Y. Yamada, Z. Zak.
We elaborated the substrate specificity of mammalian FAD synthetase
(Bowers-Komro et al. 1989
, McCormick 1964a
, McCormick 1964b
, McCormick et al. 1997
) and accomplished its partial (Gomes and McCormick 1983
) and then complete purification, again using affinity
(FMN-agarose) methods (Oka and McCormick 1987
). Further
work led to more detailed characterization of the cooperatively
interactive kinase/synthetase system and to their kinetic mechanisms
(Yamada et al. 1990
).
FMN phosphatase and FAD pyrophosphatase—S. Lee, M. Russell.
The interfering, nonspecific actions of alkaline and acid FMN
phosphatases (McCormick 1961
, McCormick and Russell 1962
) and FAD pyrophosphatase have been separated and
generally characterized as degradative hydrolases responsible for
breakdown of flavocoenzymes (Lee and McCormick 1983
).
Riboflavin side-chain oxidases—H. Chen, D. Edmondson, T. Kekelidze, C. Yang.
A bacterial side-chain oxidizing enzyme that had been called a
"hydrolase" was found by us to have relative specificity
(Yang and McCormick 1967a
), whereas another enzyme
narrowly specific for riboflavin (Kekelidze et al. 1994
,
Kekelidze et al. 1995
) has been molecularly cloned and
sequenced by us from a fungal organism (Chen and McCormick 1997a
) and found able to form both aldehyde and acid products
at the 5'-terminus (Chen and McCormick 1997b
).
Flavin metabolites and analogs—R. Addison, C. Chia, J. Chastain, J. Galloway, G. Kimmich, B. Ogunmodede, M. Oka, P. Preusch, F. Roughead, S. Tu, C. Yang, J. Zempleni.
We have helped detail the overall metabolic fate of riboflavin
(Chastain and McCormick 1987a
, Chastain and McCormick 1987b
, Chastain and McCormick 1988
,
Foley et al. 1967
, Oka and McCormick 1985
, McCormick 1975b
, McCormick 1976a
, McCormick et al. 1984
, McCormick et al. 1988
, Roughead and McCormick 1991
,
Yang and McCormick 1967b
), 8
-amino acid flavins
derived from covalent forms (Addison and McCormick 1978
,
Chia et al. 1978
), and flavin analogs (Ogunmodede and McCormick 1966
, Tu and McCormick 1969
) in
the mammal and in milk from cows (Roughead and McCormick 1990a
) and humans (Roughead and McCormick 1990b
). The finding that an 8-sulfonyl-riboflavin
appears in human urine as a result of catabolite turnover of monoamine
oxidase is noteworthy (Chastain and McCormick 1987b
).
The predominant catabolite of riboflavin to appear in plasma following
ingestion of riboflavin is the 7-hydroxy compound (Zempleni et al. 1996a
, Zempleni et al. 1996b
). The in
vivo kinetics of riboflavin absorption and disposition have been
quantitated in the normal human (Zempleni et al. 1996a
)
and in women with liver cirrhosis (Zempleni et al. 1996c
).
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Flavocoenzyme function |
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TOPABSTRACTINTRODUCTIONVitamin B-6 metabolismFlavin metabolismFlavocoenzyme functionBiotin metabolismLipoate metabolismTransport and uptake of...Metal ionsOtherREFERENCES |
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Our studies on the nature of inter- and intramolecular complexes of
flavins with purines and pyrimidines (Chassy and McCormick 1965a
, McCormick 1968a
, Roth and McCormick 1967
, Tsibris et al. 1965
) including
synthetic analogs of FAD helped elucidate the strength and types of
interactions involved, particularly within FAD. Extension of such
studies to flavin-aromatic amino acid systems (Föry et al. 1968
, Föry et al. 1970
, Getoff et al. 1978
, Johnson and McCormick 1973
,
Johnson et al. 1975
, MacKenzie et al. 1969
, McCormick 1970
, McCormick 1973
, McCormick et al. 1975
, McCormick 1977b
, Wu and McCormick 1971a
, Wu and McCormick 1971b
) and ultimately to flavoproteins
(McCormick 1970
, McCormick 1977a
,
McCormick 1977a
, McCormick and Tu 1970
,
Merrill et al. 1981b
, Shiga et al. 1975
,
Tu and McCormick 1973
, Tu and McCormick 1974
, Wu et al. 1970
) secured the expectation
that such interactions are common, particularly with tryptophanyl and
tyrosyl residues, and often account for part of the facilitated binding
of flavins to proteins.
Flavin-dependent enzymes—C. Arsenis, B. Chassy, S. Edelstein, P. Johnson, J. Koster, J. Roth, J. Tsibris, S. Tu, C. Veeger, J. Visser, F. Wu.
The specificity of coenzyme binding and function (Arsenis and McCormick 1964b
, Chassy and McCormick 1965b
,
McCormick et al. 1964
, Merrill et al. 1979b
, Roth et al. 1966
, Tsibris et al. 1966
, Visser et al. 1968
), nature of
active-site residues (Choi and McCormick 1981
,
Falk et al. 1976
, Falk and McCormick 1976
, Horiike et al. 1979b
, Koster et al. 1968
, McCormick et al. 1967
, McCormick 1970
, Tu and McCormick 1973
, Tu and McCormick 1974
, Wu et al. 1970
), and physical
properties of several flavin-dependent enzymes have been
elucidated. One common feature is the binding of the pyrimidinoid
portion of the isoalloxazine system of FMN within a cleft which often
allows projection of the dimethylbenzenoid edge toward solvent. A
prototypic example of using a coenzyme as a photochemical probe for the
active site of an enzyme was provided by our work with FAD in
D-amino acid oxidase, wherein a tyrosyl as well as lysyl
and cysteinyl residues were proven critical (Tu and McCormick 1973
). The spectrochemical effects of 8-flavin linkage to a
cysteinyl residue with monoamine oxidase were confirmed and quantitated
by our synthesis of the active-site portion of this enzyme
(Falk et al. 1976
, Falk and McCormick 1976
).
The scheme given in Figure 2
outlines central aspects of riboflavin transport, metabolism,
utilization and excretion.
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Biotin metabolism |
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TOPABSTRACTINTRODUCTIONVitamin B-6 metabolismFlavin metabolismFlavocoenzyme functionBiotin metabolismLipoate metabolismTransport and uptake of...Metal ionsOtherREFERENCES |
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We secured direct proof that biotin is biosynthesized via dethiobiotin
by use of the labeled precursor (Li et al. 1968a
,
Tepper et al. 1966
).
Metabolism—R. Brady, J. Chastain, W. Im, S. Iwahara, M. Kazarinoff, H. Lee, H. Li, L. Li, N. McCall, D. Mock, J. Roth, H. Ruis, J. Westendorf, L. Wright, J. Zempleni.
The catabolic fate of this vitamin and analogs as wholly degraded in a
pseudomonad (Brady et al. 1965
, Brady et al. 1966
, Im et al. 1970
, Im et al. 1973
, Iwahara et al. 1969
, Kazarinoff et al. 1972
, Roth et al. 1970
, Ruis et al. 1968
, Westendorf and McCormick 1980
) and partly
degraded in a fungus (Li et al. 1968b
) and the rat
(Lee et al. 1972
, Lee et al. 1973a
) was
elaborated in our laboratory. Present knowledge of the metabolism of
biotin is based on these detailed studies (McCormick 1975a
, McCormick 1976b
, McCormick and Olson 1984
, McCormick and Wright 1970
). The
identification of such metabolites in humans has now been secured
(Zempleni et al. 1996d
). A discriminating colorimetric
reaction for biotin and analogs was developed (McCormick and Roth 1970
).
Based on the numerous catabolites we have isolated and structurally
identified, an overview of events is illustrated in Figure 3.
Whereas a soil pseudomonad forced to use biotin as the sole source of
C, N, S, and energy can effect extensive degradation, including
the bicyclic ring system, mammals operate more sparingly, mainly on
side-chain ß-oxidation and oxidation of the ring sulfur.
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Lipoate metabolism |
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TOPABSTRACTINTRODUCTIONVitamin B-6 metabolismFlavin metabolismFlavocoenzyme functionBiotin metabolismLipoate metabolismTransport and uptake of...Metal ionsOtherREFERENCES |
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Similar studies on the catabolic fate of lipoate were conducted. We
detailed total degradation in a pseudomonad (Chang et al. 1975
, Furr et al. 1978
, Furr and McCormick 1978
, Shih et al. 1972
, Shih et al. 1975
) and in the rat (Harrison and McCormick 1974
, Spence and McCormick 1976
). Synthesis and
delineation of the properties of critical side-chain shortened
metabolites were also accomplished (Shih et al. 1974
) as
were HPLC chromatographic separations of metabolites (Howard and McCormick 1981
).
The routes for oxidation of side-chain and of ring sulfurs of
lipoate are shown in Figure 4.
More extensive ring degradation may occur in bacterial than mammalian
systems.
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Transport and uptake of water-soluble vitamins |
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TOPABSTRACTINTRODUCTIONVitamin B-6 metabolismFlavin metabolismFlavocoenzyme functionBiotin metabolismLipoate metabolismTransport and uptake of...Metal ionsOtherREFERENCES |
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Our studies on the means by which animals transport riboflavin have led
to detailed knowledge on selective affinity purification
(Merrill and McCormick 1978
) and properties of the avian
carrier/storage proteins (Froehlich et al. 1980
)
including its flavin-binding specificity (Choi and McCormick 1980
), the first recognition of pregnancy-induced plasma
riboflavin-carrier protein in a mammal (Merrill et al. 1979b
), and the occurrence of other cytosolic binding proteins
(Merrill et al. 1982
). Further work has led to the
identification of immunoglobulin carriers in the human (Innis et al. 1985
, Innis et al. 1986
, Merrill et al. 1981a
). Both physical (Pritchard et al. 1967
) and biological (Lee et al. 1973b
)
interactions of biotin with avidin were investigated, as was
specificity of avidin (Zempleni et al. 1996e
) and
biocytinase (McCormick 1969
).
Uptake—T. Aw, B. Bowman, D. Bowers-Komro, J. Gregory, T. Joseph, A. Kosik, Y. Suzuki, H. Tsuge, Z. Zhang.
Hepatocyte uptake of riboflavin, which is carrier-mediated but not
Na+-dependent and involves metabolic trapping by
flavokinase-catalyzed phosphorylation (Aw et al. 1983
), has been contrasted with gut (enterocyte) absorption and
with uptake by proximal tubular renal cells (Bowman et al. 1989
). The entry of pyridoxine into liver cells is similarly
insensitive to Na+ (and hence
Na+/K+ ATPase) and dependent on metabolic
trapping by pyridoxal kinase (Kozik and McCormick 1984
),
whereas uptake by renal proximal tubular cells is similar but may
involve Na+/H+ exchange and/or pH gradient
effects (Bowman and McCormick 1987
, Bowman and McCormick 1989
, McCormick 1989
). Disposition of
B-6 glucosides was shown to depend upon uptake as well as subsequent
metabolic events (Joseph et al. 1996
, Zhang et al. 1993a
). Biotin entry depends on ligandin (glutathione
S-transferase) as typical for organic acid anions (Bowers-Komro and McCormick 1985b
). Information from these studies
coupled with our knowledge of the enzymic events that occur upon entry
led to the design of vitamin analog models that exemplify
transporter-enhanced delivery of bioactive compounds
(McCormick 1994
, Zhang et al. 1993b
,
Zhang and McCormick 1991
, Zhang and McCormick 1992a
, Zhang and McCormick 1992b
).
A means by which some less-transportable compounds of
therapeutic use can be imported into cells is exemplified in
Figure 5.
A specific example we have documented is the chemical attachment of
bioactive amines to Vitamin B-6 such as to be "piggybacked" through
the B-6 transporter to be released inside of liver or kidney cells as
free amine plus coenzyme B-6.
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Metal ions |
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TOPABSTRACTINTRODUCTIONVitamin B-6 metabolismFlavin metabolismFlavocoenzyme functionBiotin metabolismLipoate metabolismTransport and uptake of...Metal ionsOtherREFERENCES |
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Not only have we shown the involvement of certain metal ions, e.g.,
Zn2+, for specific enzymes (McCormick et al. 1961
, McCormick 1962
, Sander et al. 1965
), but the general liganding properties of several
important functional groups (Griessen et al. 1971
)
including amino acids (Griesser et al. 1969
,
McCormick et al. 1969
, McCormick et al. 1974
, Sigel et al. 1969a
, Sigel et al. 1969b
, Sigel et al. 1970
, Sigel et al. 1972
, Sigel et al. 1977
, Sigel and McCormick 1971
, Sigel and McCormick 1974
,
Walker et al. 1972
), nucleotides (Sigel et al. 1967
, Sigel and McCormick 1974
), and such
vitamins as biotin (Griesser et al. 1970
,
Griesser et al. 1973
, Sigel et al. 1969c
,
Sigel et al. 1978a
, Sigel and McCormick 1974
) and lipoate (Sigel et al. 1978a
,
Sigel et al. 1978b
) have been delineated for important
cations of the Irving-Williams series. These latter studies extend
our knowledge of the possible interactions within biological metal
ion-containing systems.
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Other |
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TOPABSTRACTINTRODUCTIONVitamin B-6 metabolismFlavin metabolismFlavocoenzyme functionBiotin metabolismLipoate metabolismTransport and uptake of...Metal ionsOtherREFERENCES |
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), and M. Woods (McCormick et al. 1965
,
Woods and McCormick 1964
); dihydroorotase with
G. Sander and L. Wright (Sander et al. 1965
);
carbohydrate and lipid with J. Coniglio (Coniglio et al. 1956
); steroids with J. Feher (Feher et al. 1974
); vitamin C and D. Bowers-Komro, G. Iacobucci, G.
King, and J. Sweeney (Bowers-Komro et al. 1982
).
In summary, my associates and I have unraveled details in the
absorption, transport, cellular uptake, metabolism and function of
several water-soluble vitamins and coenzymes and have provided
additional information on metal-ion coordination. During the course
of these studies, we have pioneered in affinity chromatography
(Arsenis and McCormick 1964
, Arsenis and McCormick 1966
, Bowers-Komro et al. 1986
,
Froehlich et al. 1980
, Kazarinoff et al. 1975
, McCormick 1965
, McCormick et al. 1991
, McCormick et al. 1997
, Merrill et al. 1979a
, Merrill and McCormick 1978
,
Merrill and McCormick 1980
, Nakano and McCormick 1991a
, Oka and McCormick 1987
, Sander et al. 1966
) and immobilized enzymes (Merrill and McCormick 1979
, Tu and McCormick 1972
), established
theoretical (Horiike and McCormick 1979
, Horiike and McCormick 1980
) and experimental protocols for chemical
(Choi and McCormick 1981
, Horiike et al. 1979a
, Horiike et al. 1979b
, McCormick 1970
, Nakano et al. 1992
, Nakano and McCormick 1992
, Tsuge and McCormick 1980
) and
photochemical (Koster et al. 1968
, McCormick et al. 1967
, McCormick 1968b
, McCormick 1970
, Tu and McCormick 1973
) modifications of
enzymes, and successfully bridged information from chemical models
(spectroscopic and metal coordination compounds) to biochemical
complexes and functional systems.
Together we have followed a trail of research on cofactors which many of you and others who follow will still find rewarding.
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FOOTNOTES |
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2 Abbreviations used: FMN, flavin mononucleotide; FAD, flavin adenine dinucleotide.
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REFERENCES |
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TOPABSTRACTINTRODUCTIONVitamin B-6 metabolismFlavin metabolismFlavocoenzyme functionBiotin metabolismLipoate metabolismTransport and uptake of...Metal ionsOtherREFERENCES |
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1. Addison R., McCormick D. B. Biogenesis of flavoprotein and cytochrome components in hepatic mitochondria from riboflavin-deficient rats. Biochem. Biophys. Res. Commun. 1978;81:133-138[Medline]
2.
Arsenis C., McCormick D. B. Purification of liver flavokinase by column chromatography on flavin-cellulose compounds. J. Biol. Chem. 1964a;239:3093-3097
3. Arsenis C., McCormick D. B. Coenzyme specificity of NADPH-cytochrome c reductase for flavin phosphates. Biochim. Biophys. Acta 1964b;92:440-445
4.
Arsenis C., McCormick D. B. Purification of flavin mononucleotide dependent enzymes by column chromatography on flavin phosphate cellulose compounds. J. Biol. Chem. 1966;241:330-334
5. Aw T.-Y., Jones D. P., McCormick D. B. Uptake of riboflavin by isolated rat liver cells. J. Nutr. 1983;113:1249-1254
6. Bowers-Komro D. M., Hagen T. M., McCormick D. B. Modified purification of pyridoxamine (pyridoxine) 5'-phosphate oxidase from rabbit liver by 5'-phosphopyridoxyl affinity chromatography. Chytil F. McCormick D. B. eds. Vitamins and Coenzymes, Methods in Enzymology 1986;Vol. 122G:116-120 Academic Press Orlando, FL.
7. Bowers-Komro D. M., McCormick D. B. Mechanism and functionality of FMN in pyridoxine (pyridoxamine) 5'-phosphate oxidase. Bray R. C. Engel P. C. Mayhew S. G. eds. Flavins and Flavoproteins 1984a:581-584 Walter de Gruyter NY.
8. Bowers-Komro D. M., McCormick D. B. Steric restrictions in the active-site region of liver pyridoxamine (pyridoxine) 5'-phosphate oxidase. Evangelopoulos A. E. eds. Chemical and Biological Aspects of Vitamin B6 Catalysis. Part A 1984b,/DATE>:387-396 Alan R. Liss, Inc. NY.
9.
Bowers-Komro D. M., McCormick D. B. Pyridoxamine 5'-phosphate oxidase exhibits no specificity in prochiral hydrogen abstraction from substrate. J. Biol. Chem. 1985a;260:9580-9582
10. Bowers-Komro D. M., McCormick D. B. Biotin uptake by isolated rat liver hepatocytes. Annals of the New York Academy of Sciences 1985b;447:350-358[Medline]
11. Bowers-Komro D. M., McCormick D. B. Single- and double-headed analogs of pyridoxamine 5'-phosphate as probes for pyridoxamine 5'-phosphate utilizing enzymes. Bioorganic Chem 1987;15:224-236
12. Bowers-Komro D. M., McCormick D. B., King G. A., Sweeny J. G., Iacobucci G. A. Confirmation of 2-O-methyl ascorbic acid as the product from the enzymatic methylation of L-ascorbic acid by catechol-O-methyltransferase. Int. J. Vit. Nutr. Res. 1982;52:186-193
13. Bowers-Komro D. M., Yamada Y., McCormick D. B. Substrate specificity and variables affecting efficiency of mammalian flavin adenine dinucleotide synthetase. Biochemistry 1989;28:8439-8446[Medline]
14. Bowman B. B., McCormick D. B. Pyridoxine uptake by proximal tubular epithelial cells isolated from rat kidney. Korpela T. Christen P. eds. Biochemistry of Vitamin B6 1987:403-406 Birkhauser Basel
15. Bowman B. B., McCormick D. B. Pyridoxine uptake by rat renal proximal tubular cells. J. Nutr. 1989;119:745-749
16. Bowman B. B., McCormick D. B., Rosenberg I. H. Epithelial transport of water-soluble vitamins. Olson R. E. eds. Annual Review of Nutrition 1989;Vol. 9:187-199 Annual Reviews, Inc. Palo Alto, CA. [Medline]
17. Brady R. N., Li L. F., McCormick D. B., Wright L. D. Bacterial and enzymatic degradation of biotin. Biochem. Biophys. Res. Commun. 1965;19:777-782[Medline]
18.
Brady R. N., Ruis H., McCormick D. B., Wright L. D. Bacterial degradation of biotin. Catabolism of 14C-biotin and its sulfoxides. J. Biol. Chem. 1966;241:4717-4721
19. Chang H. H., Rozo M. L., McCormick D. B. Lipoate metabolism in Pseudomonas putida LP. Arch. Biochem. Biophys. 1975;169:244-251[Medline]
20.
Chassy B. M., Arsenis C., McCormick D. B. The effect of the side chain of flavins on reactivity with flavokinase. J. Biol. Chem. 1965;240:1338-1340
21. Chassy B. M., McCormick D. B. Structural requirements of the flavin moiety of flavin-adenine dinucleotide for intramolecular complex formation. Biochemistry 1965a;4:2612-2615[Medline]
22. Chassy B. M., McCormick D. B. Coenzyme specificity of D-amino acid oxidase for the flavin moiety of FAD. Biochim. Biophys. Acta 1965b;110:91-96[Medline]
23. Chastain J. L., McCormick D. B. Clarification and quantitation of primary (tissue) and secondary (microbial) catabolites of riboflavin which are excreted in mammalian (rat) urine. J. Nutr. 1987a;117:468-475
24.
Chastain J. L., McCormick D. B. Flavin catabolites: Identification and quantitation in human urine. Am. J. Clin. Nutr. 1987b;46:830-834
25. Chastain J. L., McCormick D. B. Characterization of a new flavin metabolite from human urine. Biochim. Biophys. Acta 1988;967:131-134[Medline]
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127. Merrill A. H., Jr, Addison R., McCormick D. B. Induction of hepatic and intestinal flavokinase after oral administration of riboflavin to riboflavin-deficient rats. Proc. Soc. Exp. Biol. Med. 1978a;158:572-574[Medline]
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146. Rasmussen K. M., Barsa P. M., McCormick D. B. Pyridoxamine (pyridoxine) 5'-phosphate oxidase activity in rat tissues during development of riboflavin or pyridoxine deficiency. Proc. Soc. Exp. Biol. Med. 1979;161:527-530[Medline]
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Shih J.C.H., Rozo M. L., Wright L. D., McCormick D. B. Characterization of the growth of Pseudomonas putida LP on lipoate and its analogues: Transport, oxidation, sulphur source, and enzyme induction. J. Gen. Microbiol. 1975;86:217-227
159. Shih J.C.H., Williams P. B., Wright L. D., McCormick D. B. Properties of lipoic acid analogs. J. Heterocycl. Chem. 1974;11:119-123
160.
Shih J.C.H., Wright L. D., McCormick D. B. Isolation, identification and characterization of a lipoate-degrading pseudomonad and of a lipoate catabolite. J. Bacteriol. 1972;112:1043-1051
161. Sigel H., Becker K., McCormick D. B. Ternary complexes in solution. Influence of 2, 2'-bipyridyl on the stability of 1:1 complexes of Co2+, Ni2+, Cu2+, and Zn2+ with hydrogen phosphate, adenosine 5'-monophosphate, and adenosine 5'-triphosphate. Biochim. Biophys. Acta 1967;148:655-664
162. Sigel H., Griesser R., McCormick D. B. On the structure of manganese(II)- and copper(II)-histidine complexes. Arch. Biochem. Biophys. 1969a;134:217-227[Medline]
163. Sigel H., Griesser R., McCormick D. B. Ternary complexes in solution. XIII. Mixed-ligand complexes of copper(II) or zinc(II) with 2,2'-bipyridyl and thioether carboxylates or some of their sulfoxide or sulfone derivatives. Inorg. Chim. Acta 1972;6:559-563
164.
Sigel H., Griesser R., Prijs B., McCormick D. B., Joiner M. "Hard and soft" behavior of Mn2+, Cu2+ and Zn2+ with respect to carboxylic acids and -oxy- or -thio-substituted carboxylic acids of biochemical significance. Arch. Biochem. Biophys. 1969b;130:514-520[Medline]
165. Sigel H., MacKenzie R. E., McCormick D. B. On the structure of copper(II)-histidine complexes. Biochim. Biophys. Acta 1970;200:411-413[Medline]
166. Sigel H., McCormick D. B. The structure of the Cu2+ L-histidine 1:2 complex in solution. J. Am. Chem. Soc. 1971;93:2041-2044[Medline]
167. Sigel H., McCormick D. B. On the discriminating behavior of metals ions and ligands with regard to their biological significance. Bunnett J. F. eds. Collected Accounts of Transition Metal Chemistry 1974 American Chemical Society Washington, D.C.
168. Sigel H., McCormick D. B., Griesser R., Prijs B., Wright L. D. Metal ion complexes with biotin and biotin derivatives. Participation of sulfur in the orientation of divalent cations. Biochemistry 1969c;8:2687-2695[Medline]
169. Sigel H., Neumann C. F., Prijs B., McCormick D. B., Falk M. C. Influence of alkyl side chains with hydroxy or thioether groups on the stability of binary and ternary copper(II)-dipeptide complexes. Inorg. Chem. 1977;16:790-796
170. Sigel H., Prijs B., McCormick D. B. Stability and structure of Cd2+ and Pb2+ complexes with biotin, lipoic acid, and some of their derivatives in solution. J. Inorg. Nucl. Chem. 1978a;40:1678-1680
171.
Sigel H., Prijs B., McCormick D. B., Shih J.C.H. Stability and structure of binary and ternary complexes of -lipoate and lipoate derivatives with Mn2+, Cu2+ and Zn2+ in solution. Arch. Biochem. Biophys. 1978b;187:208-214[Medline]
172. Spence J. T., McCormick D. B. Lipoic acid metabolism in the rat. Arch. Biochem. Biophys. 1976;174:13-19[Medline]
173.
Tepper J. P., McCormick D. B., Wright L. D. Direct evidence for the conversion of dethiobiotin to biotin in Aspergillus niger. J. Biol. Chem. 1966;241:5734-5735
174. Touster O., Mayberry R. H., McCormick D. B. The conversion of 1-13C-D-glucuronolactone to 5-13C-L-xylulose in a pentosuric human. Biochim. Biophys. Acta 1957;25:196-198
175. Tsibris J.C.M., McCormick D. B., Wright L. D. Studies on the donor–acceptor complexes relating to the intramolecular association of the riboflavin and adenosine moieties of flavin-adenine dinucleotide. Biochemistry 1965;4:504-509[Medline]
176.
Tsibris J.C.M., McCormick D. B., Wright L. D. Studies on the binding and function of flavin phosphates with flavin mononucleotide-dependent enzymes. J. Biol. Chem. 1966;241:1138-1143
177. Tsuge H., McCormick D. B. Reactivity of the sulfhydryl groups in pyridoxamine phosphate oxidase from liver. Yagi K. Yamano T. eds. Flavins and Flavoproteins 1980:517-527 Japan Scientific Society Press Tokyo.
178.
Tu S. C., McCormick D. B. The biological activity and excretion of 6,7-dimethyl-9-(-carboxyalkyl) isoalloxazines in rats. J. Nutr. 1969;97:307-310
179. Tu S. C., McCormick D. B. Insolubilized D-amino acid oxidase: Properties and potential use. Separation Sci 1972;7:403-407
180.
Tu S. C., McCormick D. B. Photoinactivation of porcine D-amino acid oxidase with flavin-adenine dinucleotide. J. Biol. Chem. 1973;248:6339-6347
181. Tu S. C., McCormick D. B. Conformation of porcine D-amino acid oxidase as studied by protein fluorescence and optical rotatory dispersion. Biochemistry 1974;13:893-899[Medline]
182. Uhler L. D., Crispen C. R., McCormick D. B. Free amino acid patterns during development of Eurosta solidaginis (Fitch). Comp. Biochem. Physiol. 1971;38:87-91
183. Visser J., McCormick D. B., Veeger C. Relation between conformation and activities of lipoamide dehydrogenase. II. Some aspects of recombination with FAD analogues. Biochim. Biophys. Acta 1968;159:257-264[Medline]
184. Walker F. A., Sigel H., McCormick D. B. Spectral properties of mixed-ligand copper(II) complexes and their corresponding binary parent complexes. Inorg. Chem. 1972;11:2756-2763
185. Westendorf J., McCormick D. B. Isolation of volatile sulfur-containing microbial catabolites of biotin. Internat. J. Vit. Nutr. Res. 1980;50:62-65
186. Woods M. N., McCormick D. B. Effects of dietary phenylalanine on activity of phenylalanine hydroxylase from rat liver. Proc. Soc. Exp. Biol. Med. 1964;116:427-430
187. Wu F.Y.H., McCormick D. B. The fluorescence quenching of aromatic amino acid and flavin portions of flavinyl peptides. Biochim. Biophys. Acta 1971a;229:440-443[Medline]
188. Wu F.Y.H., McCormick D. B. Flavin-sensitized photooxidations of tryptophan and tyrosine. Biochim. Biophys. Acta 1971b;236:479-486[Medline]
189. Wu F.Y.H., Tu S. C., Wu W. C., McCormick D. B. Characteristics of the fluorescence spectra of apoenzyme and flavin portions of D-amino acid oxidase. Biochem. Biophys. Res. Commun. 1970;41:381-385[Medline]
190. Yamada Y., Merrill A. H., , Jr & McCormick D. B. Probable reaction mechanisms of flavokinase and FAD synthetase from rat liver. Arch. Biochem. Biophys. 1990;278:125-130[Medline]
191. Yang C. S., Arsenis C., McCormick D. B. Microbiological and enzymatic assays of riboflavin analogues. J. Nutr. 1964;84:167-172[Medline]
192. Yang C. S., McCormick D. B. Substrate specificity of riboflavin hydrolase from Pseudomonas riboflavina. Biochim. Biophys. Acta 1967a;132:511-513[Medline]
193. Yang C. S., McCormick D. B. Degradation and excretion of riboflavin in the rat. J. Nutr. 1967b;93:445-453
194.
Zempleni J., Galloway J. R., McCormick D. B. Pharmacokinetics of orally and intravenously administered riboflavin in healthy humans. Am. J. Clin. Nutr. 1996a;63:54-66
195.
Zempleni J., Galloway J. R., McCormick D. B. The identification and kinetics of 7-hydroxyriboflavin (7-hydroxymethylriboflavin) in blood plasma from humans following oral administration of riboflavin supplements. Int. J. Vit. Nutr. Res. 1996b;66:151-157
196. Zempleni J., Galloway J. R., McCormick D. B. The metabolism of riboflavin in female patients with liver cirrhosis. Int. J. Vit. Nutr. Res. 1996c;66:237-243
197.
Zempleni J., McCormick D. B., Mock D. M. The identification of biotin sulfone, bisnorbiotin methyl ketone, and tetranorbiotin-1-sulfoxide in human urine. Am. J. Clin. Nutr. 1996d;65:508-511
198. Zempleni J., McCormick D. B., Stratton S. L., Mock D. M. Lipoic acid (thioctic acid) analogs, tryptophan analogs, and urea do not interfere with the assay of biotin and biotin metabolites by high-performance liquid chromatography/avidin-binding assay. J. Nutr. Biochem. 1996e;7:518-523
199. Zhang Z., Gregory J. E., , III & McCormick D. B. Uptake and metabolism of pyridoxine-5'-ß-D-glucoside by isolated rat liver cells. J. Nutr. 1993a;123:85-89
200.
Zhang Z., McCormick D. B. Uptake of N-(4'-pyridoxyl) amines and release of amines by renal cells: A model for transporter-enhanced delivery of bioactive compounds. Proc. Natl. Acad. Sci. (USA) 1991;88:10407-10410
201. Zhang Z., McCormick D. B. Uptake and metabolism of N-(4'-pyridoxyl)amines by isolated rat liver cells. Arch. Biochem. Biophys. 1992a;294:394-397[Medline]
202. Zhang Z., McCormick D. B. Uptake and metabolism of 4'(N)-substituted pyridoxamines by cells from the liver and kidneys of rats. Kobayashi T. eds. 1st Internat’l. Congress on Vitamin and Biofactors in Life Science 1992b:208-211 Center for Academic Publications Osaka, Japan.
203. Zhang Z., Smith E., Surowiec S. M., Merrill A. H., Jr, McCormick D. B. Synthesis of N-(4'-pyridoxyl)-sphingosine and its uptake and metabolism by isolated cells. Membrane Biochem 1993b;10:53-59
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