منابع مشابه
Reduction kinetics of bacterial cytochromes c2.
In a continuing effort to understand the mechanism of electron transfer by c-type cytochromes we have extended our investigations of the oxidation and reduction of Rhodospirillum rubrum cytochrome ct. We have utilized the oxidant, oxidized azurin, and the reductants SOP-, S204*-, sodium ascorbate, and reduced azurin. The results of these studies demonstrate that, as found previously with the ir...
متن کاملThiosulphate oxidation and cytochromes in Thiobacillus X. 1. Fractionation of bacterial extracts and properties of cytochromes.
In a preliminary communication (Trudinger, 1958) the separation of some soluble cytochromes of the autotrophic sulphur bacterium Thiobacillue X was briefly reported. Addition of thiosulphate to intact cells results in the rapid reduction of the cytochromes and the present work was undertaken to attempt to characterize the cytochromes and to obtain some information on the electron-transport chai...
متن کاملRapid electron exchange between surface-exposed bacterial cytochromes and Fe(III) minerals.
The mineral-respiring bacterium Shewanella oneidensis uses a protein complex, MtrCAB, composed of two decaheme cytochromes, MtrC and MtrA, brought together inside a transmembrane porin, MtrB, to transport electrons across the outer membrane to a variety of mineral-based electron acceptors. A proteoliposome system containing a pool of internalized electron carriers was used to investigate how th...
متن کاملPhysiological function and catalytic versatility of bacterial multihaem cytochromes c involved in nitrogen and sulfur cycling.
Bacterial MCCs (multihaem cytochromes c) represent widespread respiratory electron-transfer proteins. In addition, some of them convert substrates such as nitrite, hydroxylamine, nitric oxide, hydrazine, sulfite, thiosulfate or hydrogen peroxide. In many cases, only a single function is assigned to a specific MCC in database entries despite the fact that an MCC may accept various substrates, th...
متن کاملPreparation of human metabolites of propranolol using laboratory-evolved bacterial cytochromes P450.
Testing the toxicities and biological activities of the human metabolites of drugs is important for development of safe and effective pharmaceuticals. Producing these metabolites using human cytochrome P450s is difficult, however, because the human enzymes are costly, poorly stable, and slow. We have used directed evolution to generate variants of P450 BM3 from Bacillus megaterium that function...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Bacteriological Reviews
سال: 1954
ISSN: 0005-3678
DOI: 10.1128/br.18.2.106-130.1954