Michael D Clay
Overview
Explore the profile of Michael D Clay including associated specialties, affiliations and a list of published articles.
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Articles
15
Citations
299
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Recent Articles
1.
Bong Y, Song S, Nazor J, Vogel M, Widegren M, Smith D, et al.
J Org Chem
. 2018 Jun;
83(14):7453-7458.
PMID: 29932340
A wild-type Baeyer-Villiger monooxygenase was engineered to overcome numerous liabilities in order to mediate a commercial oxidation of pyrmetazole to esomeprazole, using air as the terminal oxidant in an almost...
2.
Jensen K, Bell 3rd C, Clay M, Solomon E
J Am Chem Soc
. 2009 Aug;
131(34):12155-71.
PMID: 19663382
We have performed a systematic study of chemically possible peroxo-type intermediates occurring in the non-heme di-iron enzyme class Ia ribonucleotide reductase, using spectroscopically calibrated computational chemistry. Density functional computations of...
3.
Fox R, Clay M
Trends Biotechnol
. 2009 Feb;
27(3):137-40.
PMID: 19193465
Recent attention has been paid to the inadequacy of using the ratio Vmax/KM as a measure of enzyme performance, particularly in the context of industrial biocatalysis. This can lead to...
4.
Mitic N, Clay M, Saleh L, Bollinger Jr J, Solomon E
J Am Chem Soc
. 2007 Jul;
129(29):9049-65.
PMID: 17602477
Spectroscopic and electronic structure studies of the class I Escherichia coli ribonucleotide reductase (RNR) intermediate X and three computationally derived model complexes are presented, compared, and evaluated to determine the...
5.
Yang T, McNaughton R, Clay M, Jenney Jr F, Krishnan R, Kurtz Jr D, et al.
J Am Chem Soc
. 2006 Dec;
128(51):16566-78.
PMID: 17177406
Superoxide reductase (SOR) and P450 enzymes contain similar [Fe(N)4(SCys)] active sites and, although they catalyze very different reactions, are proposed to involve analogous low-spin (hydro)peroxo-Fe(III) intermediates in their respective mechanisms...
6.
Decker A, Clay M, Solomon E
J Inorg Biochem
. 2006 Mar;
100(4):697-706.
PMID: 16510189
High-valent iron-oxo intermediates are known or believed to be key oxidizing species in the catalytic mechanisms of many mononuclear and binuclear non-heme iron enzymes. So far only limited experimental data...
7.
Clay M, Yang T, Jenney Jr F, Kung I, Cosper C, Krishnan R, et al.
Biochemistry
. 2006 Jan;
45(2):427-38.
PMID: 16401073
We have added cyanide to oxidized 1Fe and 2Fe superoxide reductase (SOR) as a surrogate for the putative ferric-(hydro)peroxo intermediate in the reaction of the enzymes with superoxide and have...
8.
Duin E, Signor L, Piskorski R, Mahlert F, Clay M, Goenrich M, et al.
J Biol Inorg Chem
. 2004 May;
9(5):563-76.
PMID: 15160314
Methyl-coenzyme M reductase (MCR) catalyzes the methane-forming step in methanogenic archaea. It contains the nickel porphinoid F(430), a prosthetic group that has been proposed to be directly involved in the...
9.
Clay M, Emerson J, Coulter E, Kurtz Jr D, Johnson M
J Biol Inorg Chem
. 2003 May;
8(6):671-82.
PMID: 12764688
The electronic and vibrational properties of the [Fe(His)(4)(Cys)] site (Center II) responsible for catalysis of superoxide reduction in the two-iron superoxide reductase (2Fe-SOR) from Desulfovibrio vulgaris have been investigated using...
10.
Clay M, Cosper C, Jenney Jr F, Adams M, Johnson M
Proc Natl Acad Sci U S A
. 2003 Mar;
100(7):3796-801.
PMID: 12655067
Nitric oxide (NO) has been used as a substrate analog to explore the structural and electronic determinants of enzymatic superoxide reduction at the mononuclear iron active site of Pyrococcus furiosus...