Reactivity of Reduced [2Fe-2S] Ferredoxins Parallels Host Susceptibility to Nitroimidazoles
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چکیده
منابع مشابه
Reactivity of reduced [2Fe-2S] ferredoxins parallels host susceptibility to nitroimidazoles.
The kinetics of the electron transfer reaction between reduced [2Fe-2S] ferredoxins and select nitroimidazole antimicrobial agents is reported. The ferredoxins from the protozoan Trichomonas vaginalis and the cyanobacterium Anabaena sp. strain 7120 were studied because they are the proximal electron donors to nitroimidazoles in these two organisms with significantly different nitroimidazole sus...
متن کاملStructure-function studies of [2Fe-2S] ferredoxins.
The ability to overexpress [2Fe-2S] ferredoxins in Escherichia coli has opened up exciting research opportunities. High-resolution x-ray structures have been determined for the wild-type ferredoxins produced by the vegatative and heterocyst forms of Anabaena strain 7120 (in their oxidized states), and these have been compared to structural information derived from multidimensional, multinuclear...
متن کاملPrimary structure of protein B from Pseudomonas putida, member of a new class of 2Fe-2S ferredoxins.
The primary structure of the 2Fe-2S ferredoxin (protein B) from the benzene dioxygenase system of Pseudomonas putida strain NCIB 12190 was determined by gas-phase sequencing of the protein and its fragments. Fast atom bombardment mass spectrometry indicated a molecular mass of 11,860 Da. The sequence contained five cysteine residues, four of which would be required to coordinate the iron-sulphu...
متن کاملAn Analysis of g Strain in the EPR of Two [2Fe-2S] Ferredoxins. Evidence for a Protein Rigidity Model
Replacing current notions of a pammagnetic center in a metalloprotein as a single entity in vivo with the more real&tic concept of an ensemble of spin systems, each uniquely dishded by its own surrounding protein leads to a rigorous description of the spectroscopic factor, g, as a random variable whose statistical properties contain information on the rigidity of the protein. Generation of a co...
متن کاملIdentification of [2Fe-2S] clusters in microbial ferrochelatases.
The terminal enzyme of heme biosynthesis, ferrochelatase (EC 4.99.1.1), catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme. Prior to the present work, [2Fe-2S] clusters have been identified and characterized in animal ferrochelatases but not in plant or prokaryotic ferrochelatases. Herein we present evidence that ferrochelatases from the bacteria Caulobacter cresce...
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ژورنال
عنوان ژورنال: Antimicrobial Agents and Chemotherapy
سال: 2003
ISSN: 0066-4804,1098-6596
DOI: 10.1128/aac.47.1.302-308.2003