نتایج جستجو برای: cytochromes

تعداد نتایج: 26574  

2012
Ying Liu Daniel R Bond

So close, but yet so far: G. sulfurreducens c-type cytochromes become reduced as biofilms grow on electrodes beyond a few cell thicknesses, even if the electrode is poised well above the potential required to oxidize all cytochromes. Cytochrome redox state also lags behind rapid potential changes during voltammetry, but only when the films are multiple cell layers thick, as would be expected if...

Journal: :Journal of Biological Chemistry 1968

Journal: :The Journal of biological chemistry 1970
E Margoliash A Nisonoff M Reichlin

The production of antibodies by rabbits in response to monomeric preparations of human, Macaca mulatta, and horse cytochromes c, incorporated in complete Freund’s adjuvant, is described. These antibodies precipitate with the monomeric homologous antigens, whereas no such precipitates occurred with antisera elicited by monomeric preparations of the kangaroo (Macropus canguru), turkey, and tuna p...

Journal: :The Biochemical journal 1983
J A Ward C N Hunter O T Jones

Several strains and mutants of Rhodopseudomonas sphaeroides can be grown anaerobically in the dark in the presence of dimethyl sulphoxide as an electron acceptor. During adaptation to this fermentative mode of growth, two major c-type cytochromes are synthesized, one with Mr 45 000 and the second with Mr 20 000 and a midpoint potential of +120 mV. These cytochromes are barely detectable in memb...

Journal: :The Biochemical journal 2004
James W A Allen Michael L Ginger Stuart J Ferguson

The c-type cytochromes are characterized by the covalent attachment of haem to the polypeptide via thioether bonds formed from haem vinyl groups and, normally, the thiols of two cysteines in a CXXCH motif. Intriguingly, the mitochondrial cytochromes c and c1 from two euglenids and the Trypanosomatidae contain only a single cysteine within the haem-binding motif (XXXCH). There are three known di...

Journal: :Applied and environmental microbiology 2001
A I Tsapin I Vandenberghe K H Nealson J H Scott T E Meyer M A Cusanovich E Harada T Kaizu H Akutsu D Leys J J Van Beeumen

Two abundant, low-redox-potential cytochromes c were purified from the facultative anaerobe Shewanella oneidensis strain MR1 grown anaerobically with fumarate. The small cytochrome was completely sequenced, and the genes coding for both proteins were cloned and sequenced. The small cytochrome c contains 91 residues and four heme binding sites. It is most similar to the cytochromes c from Shewan...

Journal: :The Biochemical journal 1975
G W Pettigrew I Aviram A Schejter

Cytochrome c-557 from Crithidia oncopelti and cytochrome c-558 from Euglena gracilis are mitochondrial cytochromes c that have an atypical haem-binding site. It was of interest to know whether the loss of one thioether bond affected the physicochemical properties of these cytochromes. The thermodynamic parameters of the redox potential were measured. The reaction with imidazole, the kinetics an...

Journal: :Journal of bacteriology 1997
K K Gabbert B S Goldman R G Kranz

The photosynthetic bacterium Rhodobacter capsulatus synthesizes c-type cytochromes under a variety of growth conditions. For example, under aerobic growth, c-type cytochromes are synthesized as part of an electron transport pathway, using oxygen as the terminal electron acceptor. Anaerobically in the light, R. capsulatus requires cytochrome bc1 and other c-type cytochromes for the photosyntheti...

2015
Marcus J. Edwards Gaye F. White Michael Norman Alice Tome-Fernandez Emma Ainsworth Liang Shi Jim K. Fredrickson John M. Zachara Julea N. Butt David J. Richardson Thomas A. Clarke

Extracellular microbe-mineral electron transfer is a major driving force for the oxidation of organic carbon in many subsurface environments. Extracellular multi-heme cytochromes of the Shewenella genus play a major role in this process but the mechanism of electron exchange at the interface between cytochrome and acceptor is widely debated. The 1.8 Å x-ray crystal structure of the decaheme Mtr...

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