Results 191 to 200 of about 160,314 (244)

Supporting activities of cognate redox partners for sterol-metabolizing P450 enzymes in Mycobacterium neoaurum. [PDF]

J Biol Chem
Liu Y, Zhao Y, Sun W, Li N, Pan Y, Ma L, Li S.   +6 more
europepmc   +1 more source

Human xenobiotic metabolism proteins have full-length and split homologs in the gut microbiome. [PDF]

G3 (Bethesda)
Rendina M, Turnbaugh PJ, Bradley PH.
europepmc   +1 more source

Conserved multiheme cytochrome machinery for extracellular electron transfer is widespread and transcriptionally active across deep peat profiles

Fiorito G, Priest T, Dede B, Zehnle H, Schroth MH, Sander M, Schoelmerich MC.   +6 more
europepmc   +1 more source

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The Relation of Diaphorase and Cytochrome Reductase

Biochimica Et Biophysica Acta, 1960
Abstract Diaphorase and cytochrome reductase have been extracted differentially from a pig heart-muscle preparation under various conditions. The results indicate that there is no foundation for the suggestion that diaphorase is a degraded form of cytochrome reductase.
V Massey
exaly   +3 more sources

Reduction of Cytochrome b5 by NADPH–Cytochrome P450 Reductase

Archives of Biochemistry and Biophysics, 2005
The reduction of mammalian cytochrome b5 (b5) by NADPH-cytochrome P450 (P450) reductase is involved in a number of biological reactions. The kinetics of the process have received limited consideration previously, and a combination of pre-steady-state (stopped-flow) and steady-state approaches was used to investigate the mechanism of b5 reduction.
Frederick Peter Guengerich
exaly   +3 more sources

NADPH-cytochrome P450 reductase

Archives of Biochemistry and Biophysics, 1976
Abstract The rate of reduction of cytochrome P450 in hepatic microsomes in the presence of NADPH has been measured with a dual wavelength stopped-flow spectrophotometer. The results obtained, with microsomes prepared from phenobarbital-pretreated rats, indicate that the reduction process is biphasic and most probably composed of two concurrent first ...
T, Matsubara, J, Baron, L L, Peterson, J A, Peterson   +3 more
openaire   +2 more sources

Structure of cytochrome c nitrite reductase

Nature, 1999
The enzyme cytochrome c nitrite reductase catalyses the six-electron reduction of nitrite to ammonia as one of the key steps in the biological nitrogen cycle, where it participates in the anaerobic energy metabolism of dissimilatory nitrate ammonification.
Einsle, Oliver, Messerschmidt, Albrecht, Stach, Petra, Bourenkov, Gleb P., Bartunik, Hans D., Huber, Robert, Kroneck, Peter M. H.   +6 more
openaire   +4 more sources

Microsomal DPNH cytochrome C reductase

Biochimica et Biophysica Acta, 1958
Publisher Summary This chapter discusses the microsomal DPNH-cytochrome c reductase. Enzymatic activity at 38° was measured spectrophotometrically by following the rate of reduction of cytochrome c at 550 mμ. Protein concentration is determined by the biuret method, with deoxycholate added to a final concentration of 1%.
N, PENN, B, MACKLER
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Tocopherol as an Activator of Cytochrome C Reductase

Science, 1955
Since itsdiscovery morethan30years agoasafat-soluble factor necessary for reproduction intherat, vitamin E(a-, 0-, y-,and8-tocopherols) hasbeenassociated withawidevariety ofbiological processes. A numberofrecent reviews (1-3)havesummarized thecurrent status ofourknowledge ofthevitamin.
A, NASON, I R, LEHMAN
openaire   +2 more sources

The mechanism of cytochrome b5 reduction by NADPH-cytochrome c reductase

Archives of Biochemistry and Biophysics, 1974
Abstract Microsomal suspensions of liver can catalyze the reduction of cytochrome b 5 by the membrane-bound NADPH-cytochrome c reductase but the highly purified NADPH-cytochrome c reductase obtained by lipase solubilization does not reduce cytochrome b 5 under normal assay conditions.
R A, Prough, B S, Masters
openaire   +2 more sources