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IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins
TLDR
The finding that IscR activity is decreased in strain backgrounds in which Fe-S cluster assembly is impaired suggests that this protein may be part of a novel autoregulatory mechanism that senses the Fe-sulfur cluster assembly status of cells. Expand
The Radical SAM Superfamily.
TLDR
The radical S-adenosylmethionine (SAM) superfamily currently comprises more than 2800 proteins with the amino acid sequence motif CxxxCxxC unaccompanied by a fourth conserved cysteine, which participates in more than 40 distinct biochemical transformations. Expand
Ornithine cyclodeaminase: structure, mechanism of action, and implications for the mu-crystallin family.
TLDR
The structure revealed that the substrate carboxyl group interacts with the side chains of Arg45, Lys69, and Arg112, and the ammonia leaving group hydrogen bonds to the side chain of Asp228 and the site of hydride transfer is 3.8 A from C4 of the nicotinamide. Expand
Mechanistic roles of tyrosine 149 and serine 124 in UDP-galactose 4-epimerase from Escherichia coli.
TLDR
It is concluded that Tyr 149 provides the driving force for general acid-base catalysis, with Ser 124 playing an important role in mediating proton transfer. Expand
The x-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale.
TLDR
The structure of the SAM/[4 Fe-4S] complex confirms and extends conclusions from spectroscopic studies of LAM and shows selenium in Se-adenosyl-L-selenomethionine poised to ligate the unique iron in the [4Fe- 4S] cluster upon electron transfer and radical formation. Expand
Structural analysis of the H166G site-directed mutant of galactose-1-phosphate uridylyltransferase complexed with either UDP-glucose or UDP-galactose: detailed description of the nucleotide sugar
TLDR
The mutant protein structures presented here represent valid models for understanding substrate recognition and binding in the native galactose-1-phosphate uridylyltransferase. Expand
A new iron-sulfur flavoprotein of the respiratory chain. A component of the fatty acid beta oxidation pathway.
TLDR
It is concluded that in vitro the Fe-S flavoprotein is an electron acceptor for ETF and a Q-l reductase and also functions in viva as an electron carrier in fatty acid oxidation. Expand
S-Adenosylmethionine-dependent reduction of lysine 2,3-aminomutase and observation of the catalytically functional iron-sulfur centers by electron paramagnetic resonance.
TLDR
AdoMet is shown to interact with the iron-sulfur cluster at the active site of Clostridial lysine 2,3-aminomutase, which accounts for the results of tritium tracer experiments, explains the radical rearrangement mechanism, and rationalizes the roles of AdoMet and the [4Fe-4S] cluster in the reaction. Expand
Enantiomeric free radicals and enzymatic control of stereochemistry in a radical mechanism: the case of lysine 2,3-aminomutases.
TLDR
Evidence indicates that the opposite stereochemistry displayed by E. coli LAM is determined by the conformation of the lysine side chain in the active site, as in the action of the clostridial enzyme. Expand
Interaction of ubisemiquinone with a paramagnetic component in heart tissue.
TLDR
It is suggested that the unidentified signal arises from an interaction of ubisemiquinone and a second paramagnetic species, which appears to be of the magnetic dipole-dipole type, but it is not certain whether there is also a contribution from spin exchange coupling. Expand
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