نتایج جستجو برای: ferredoxin gene
تعداد نتایج: 1146662 فیلتر نتایج به سال:
Sphingomonas sp. strain A4 is capable of utilizing acenaphthene as its sole carbon and energy source. To isolate the genes responsible for acenaphthene degradation, transposon mutagenesis was performed on strain A4 and four mini-Tn5-inserted mutants lacking the ability to utilize acenaphthene were isolated. In three of the four mini-Tn5 inserted mutants, the mini-Tn5s were inserted into the sam...
Photosynthetic microorganisms typically have multiple isoforms of the electron transfer protein ferredoxin, although we know little about their exact functions. Surprisingly, a Chlamydomonas reinhardtii mutant null for the ferredoxin-5 gene (FDX5) completely ceased growth in the dark, with both photosynthetic and respiratory functions severely compromised; growth in the light was unaffected. Th...
A second ferredoxin protein was isolated from the thermophilic anaerobic bacterium Clostridium thermoaceticum and termed ferredoxin II. This ferredoxin was found to contain 7.9 +/- 0.3 iron atoms and 7.4 +/- 0.4 acid-labile sulfur atoms per mol of protein. Extrusion studies of the iron-sulfur centers showed the presence of two [Fe4-S4] centers per mol of protein and accounted for all of the iro...
Chloroplasts photochemically reduce 1,1'-trimethylene-2,2'-dipyridylium dibromide and concurrently form adenosine triphosphate. Reduced trimethylene dipyridyl in darkness will reduce spinach ferredoxin, Clostridium pasteurianum ferredoxin, nicotinamide-adenine dinucleotide phosphate, and other viologen-type dyes.
A new type of ferredoxin was isolated from Azotobacter vinelandii cells. The protein was able to replace the native chloroplast ferredoxin in the photoreduction of nicotinamide adenine dinucleotide phosphate (NADP) and functioned as a reductant for the Azotobacter nitrogenase.
Moorella thermoacetica was long the only model organism used to study the biochemistry of acetogenesis from CO(2). Depending on the growth substrate, this Gram-positive bacterium can either form H(2) or consume it. Despite the importance of H(2) in its metabolism, a hydrogenase from the organism has not yet been characterized. We report here the purification and properties of an electron-bifurc...
Glutamate synthases (GOGAT) were analyzed to identify the functional binding domains of the substrate (glutamine) and cofactors (FMN, NAD(P)H, FAD, [3Fe-4S] and [4Fe-4S] clusters and ferredoxin) on this enzyme. The published amino acid sequences of six different NAD(P)Hdependent GOGATs (NAD(P)H-GOGAT) and ten different ferredoxin-dependent GOGATs (Fd-GOGAT) were used for this analysis. The amin...
Heme A is a prosthetic group of all eukaryotic and some prokaryotic cytochrome oxidases. This heme differs from heme B (protoheme) at two carbon positions of the porphyrin ring. The synthesis of heme A begins with farnesylation of the vinyl group at carbon C-2 of heme B. The heme O product of this reaction is then converted to heme A by a further oxidation of a methyl to a formyl group on C-8. ...
The ability of several low-potential redox proteins to mediate electron transfer between Clostridium pasteurianum pyruvate-ferredoxin oxidoreductase and hydrogenase has been evaluated in a coupled enzymatic assay. The active electron mediators, whatever their structure, must have a reduction potential compatible with the two enzymes, but for proteins of similar potentials, a marked specificity ...
نمودار تعداد نتایج جستجو در هر سال
با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید