Results 31 to 40 of about 31,102 (142)

13C-Methyl isocyanide as an NMR probe for cytochrome P450 active site [PDF]

open access: yes, 2009
The cytochromes P450 (CYPs) play a central role in many biologically important oxidation reactions, including the metabolism of drugs and other xenobiotic compounds.
Im, Sang-Choul   +4 more
core   +2 more sources

Ultrastructure and biochemical function of the mitochondria in respiratory-deficient mutant yeast induced by 4-nitroquinoline nitrogen oxide [PDF]

open access: yes, 1969
1. A respiratory-deficient mutant strain of yeast was obtained from wild strain of Saccharomyces servisiae by treatment with 4-nitroquinoline N-oxide. Ultrastructure and function of the wild or mutant strains and the mitochondrial fractions isolated from
Goto, Nobuyuki   +3 more
core   +1 more source

A functional description of CymA, an electron-transfer hub supporting anaerobic respiratory flexibility in Shewanella [PDF]

open access: yes, 2012
CymA (tetrahaem cytochrome c) is a member of the NapC/NirT family of quinol dehydrogenases. Essential for the anaerobic respiratory flexibility of shewanellae, CymA transfers electrons from menaquinol to various dedicated systems for the reduction of ...
Butt, Julea N.   +10 more
core   +1 more source

Editing of Cytochrome b mRNA inPhysarum Mitochondria [PDF]

open access: yesJournal of Biological Chemistry, 1999
The reading frame in the mRNA for the cytochrome b apoprotein in mitochondria of Physarum polycephalum is created by the insertion of 43 nucleotides in the mRNA relative to the mtDNA sequence encoding it (RNA editing). Most of these insertions (31) are single cytidines; however, single uridines are inserted at six sites, and the dinucleotides, CU and ...
Wang, S.S., Mahendran, R., Miller, D.L.
openaire   +3 more sources

Characterisation of MtoD from Sideroxydans lithotrophicus: a cytochrome c electron shuttle used in lithoautotrophic growth [PDF]

open access: yes, 2015
The autotrophic Sideroxydans lithotrophicus ES-1 can grow by coupling the oxidation of ferrous iron to the reduction of oxygen. Soluble ferrous iron is oxidised at the surface of the cell by an MtoAB porin-cytochrome complex that functions as an electron
Beckwith, Chris   +6 more
core   +2 more sources

Characterization of an electron conduit between bacteria and the extracellular environment [PDF]

open access: yes, 2009
A number of species of Gram-negative bacteria can use insoluble minerals of Fe(III) and Mn(IV) as extracellular respiratory electron acceptors. In some species of Shewanella, deca-heme electron transfer proteins lie at the extracellular face of the outer
Alex S. Beliaev   +18 more
core   +4 more sources

Successive translocation into and out of the mitochondrial matrix [PDF]

open access: yes, 1987
We investigated the import and sorting pathways of cytochrome b2 and cytochrome c1, which are functionally located in the intermembrane space of mitochondria.
Alt   +67 more
core   +1 more source

Apocytochrome c [PDF]

open access: yes, 1990
The cytochrome c import pathway differs markedly from the general route taken by the majority of other imported proteins, which is characterized by the import involvement of namely, surface receptors, the general insertion protein (GIP), contact sites ...
Berkout   +68 more
core   +1 more source

Isolation of oligomycin-sensitive adenosine triphosphatase from beef heart mitochondria and analysis of its fine structure [PDF]

open access: yes, 1967
1. An oligomycin -sensitive ATPase was isolated and partially purified from beef heart mitochondria. The specific activity of ATPase sensitive to oligomycin of the fraction was five to eight times that of aged mitochondrial or of DNP-induced ...
Hayashi, Hideo   +4 more
core   +1 more source

Using Resonance Raman Cross-section Data to Estimate the Spin State Populations of Cytochromes P450 [PDF]

open access: yes, 2013
The cytochromes P450 (CYPs) are heme proteins responsible for the oxidation of xenobiotics and pharmaceuticals and the biosynthesis of essential steroid products.
Kincaid, James R.   +2 more
core   +2 more sources

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