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Open AccessJournal ArticleDOI

The Carbon Monoxide-binding Pigment of Liver Microsomes I. EVIDENCE FOR ITS HEMOPROTEIN NATURE

Tsuneo Omura, +1 more
- 01 Jul 1964 - 
- Vol. 239, Iss: 7, pp 2370-2378
TLDR
The present paper gives a detailed account of the investigations on rabbit liver microsomes and crude microsomal digests, which have led to postulate the hemoprotein nature of the pigment.
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This article is published in Journal of Biological Chemistry.The article was published on 1964-07-01 and is currently open access. It has received 11895 citations till now. The article focuses on the topics: Carbon monoxide binding & Microsome.

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Citations
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Journal ArticleDOI

Immunochemical evidence for the participation of cytochrome b5 in microsomal stearyl-CoA desaturation reaction

TL;DR: Results confirmed the previous conclusion that the reducing equivalent for the desaturation reaction is transferred from NAD(P)H to the cyanidesensitive factor mainly via cytochrome b 5 in the microsomal membranes.
Journal ArticleDOI

Cytochrome P-450 as a microsomal peroxidase in steroid hydroperoxide reduction.

TL;DR: Investigation of the decomposition of steroid and other organic hydroperoxides by the microsomal fractions of rat liver and bovine adrenal cortex revealed that the 17α-hydroperoxide derivatives of progesterone, pregnenolone, and allopregnanolone were very effective substrates.
Journal ArticleDOI

Cloning, expression and characterisation of CYP102A7, a self-sufficient P450 monooxygenase from Bacillus licheniformis

TL;DR: Comparison of a CYP102A2 homology model with the CYP 102A1 crystal structure revealed significant differences in the substrate access channels, which might explain the differences inThe catalytic properties of these two enzymes.
Journal ArticleDOI

Rotation of cytochrome P-450. I. Investigations of protein-protein interactions of cytochrome P-450 in phospholipid vesicles and liver microsomes.

TL;DR: The measurements were used to investigate intermolecular interactions of cytochrome P-450 and found that in vesicles of a high lipid to protein ratio, the residual time-independent normalized anisotropy, r (infinity)/r (0), reached a limiting low value, implying that all cyto Chrome P- 450 was rotating.
Journal ArticleDOI

Mechanism-based inactivation of P450 2A6 by furanocoumarins.

TL;DR: The results suggest that relative to the cell system, more reactive intermediates can escape, rather than bind to, the active site of purified reconstituted P450 2A6.
References
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Journal Article

Protein Measurement with the Folin Phenol Reagent

TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
Journal ArticleDOI

The Carbon Monoxide-binding Pigment of Liver Microsomes II. SOLUBILIZATION, PURIFICATION, AND PROPERTIES

TL;DR: The present paper gives a detailed account of the investigations on rabbit liver microsomes and crude microsomal digests, which have led to postulate the hemoprotein nature of the pigment.
Journal ArticleDOI

Hepatic Triphosphopyridine Nucleotide-Cytochrome c Reductase: Isolation, Characterization, and Kinetic Studies

TL;DR: Evidence is presented which suggests that this enzyme participates in a microsomal elect,ron transport system which does not include cytochrome c and kinetic evidence has been obtained which allows certain conclusions to be drawn concerning the mechanism of catalysis by this enzyme.
Journal ArticleDOI

Microsomal triphosphopyridine nucleotide-cytochrome c reductase of liver.

TL;DR: The biological role of reduced triphosphopyridine nucleotide (TPNH) and the metabolic pathways of its hydrogen atom and electron appear to be fundamentally different from those of reduced diphosphipyridineucleotide (DPNH).
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