Purification and properties of a membrane-bound NADH-cytochrome-b5 reductase from erythrocytes of the sipunculid worm, Phascolopsis gouldii
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference27 articles.
1. A cytochrome b5 from erythrocytes of Phascolopsis gouldii. One component of a potential system for reduction of methemerythrin in vivo
2. Cytochrome b5 and NADH-cytochrome-b5 reductase from sipunculan erythrocytes; a methemerythrin reduction system from Phascolopsis gouldii
3. On the Mechanism of Dehydrogenation of Fatty Acyl Derivatives of Coenzyme A
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1. Methemoglobin reduction by NADH–cytochrome b5 reductase in Propsilocerus akamusi larvae;Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology;2015-07
2. Purified NADH-cytochrome b5 reductase is a novel superoxide anion source inhibited by apocynin: sensitivity to nitric oxide and peroxynitrite;Free Radical Biology and Medicine;2014-08
3. P450 monooxygenases (P450ome) of the model white rot fungusPhanerochaete chrysosporium;Critical Reviews in Microbiology;2012-05-25
4. Cytochrome b5 reductase–cytochrome b5 as an active P450 redox enzyme system in Phanerochaete chrysosporium: Atypical properties and in vivo evidence of electron transfer capability to CYP63A2;Archives of Biochemistry and Biophysics;2011-05
5. Oxymyohemerythrin: discriminating between O2 release and autoxidation;Journal of Inorganic Biochemistry;2000-10
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