The Carbon Monoxide-binding Pigment of Liver Microsomes I. EVIDENCE FOR ITS HEMOPROTEIN NATURE
Tsuneo Omura,Ryo Sato +1 more
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.About:
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.read more
Citations
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Journal ArticleDOI
A Single Mutation in Cytochrome P450 BM3 Changes Substrate Orientation in a Catalytic Intermediate and the Regiospecificity of Hydroxylation
Catherine F. Oliver,Sandeep Modi,Michael J. Sutcliffe,W. U. Primrose,Lu-Yun Lian,Gordon C. K. Roberts +5 more
TL;DR: Analysis of the products of the action of the enzyme on laurate and myristate showed that the mutant catalyzed hydroxylation almost exclusively at the omega position, in marked contrast to the wild-type enzyme, with which no hydroxyation at this position was observed.
Journal ArticleDOI
Monooxygenase activity of human liver in microsomal fractions of needle biopsy specimens.
TL;DR: Methods are described for the determination of mixed function oxidase activity in microsomal fractions from percutaneous needle biopsies of human liver and the presence of liver disease caused a significant decrease in AHH activity and cytochrome P-450 content.
Journal ArticleDOI
Production of the sesquiterpenoid (+)-nootkatone by metabolic engineering of Pichia pastoris.
Tamara Wriessnegger,Peter Andreas Augustin,Matthias Engleder,Erich Leitner,Monika Müller,Iwona Kaluzna,Martin Schürmann,Daniel Mink,Günther Zellnig,Helmut Schwab,Harald Pichler +10 more
TL;DR: Intracellular production of (+)-valencene by co-expression of valencene synthase from Callitropsis nootkatensis resolved the phase-transfer issues of (+-valencenes.
Journal ArticleDOI
CYP153A6, a Soluble P450 Oxygenase Catalyzing Terminal-Alkane Hydroxylation
TL;DR: Spectroscopic binding studies showed that C6-to-C11 aliphatic alkanes bind in the active site with Kd values varying from approximately 20 nM to 3.7 microM, suggesting that the substrate-binding pocket is shaped such that linear alkanes are preferred.
Journal ArticleDOI
CYP719B1 is salutaridine synthase, the C-C phenol-coupling enzyme of morphine biosynthesis in opium poppy
Andreas Gesell,Megan Rolf,Joerg Ziegler,Maria Luisa Díaz Chávez,Maria Luisa Díaz Chávez,Fong Chin Huang,Toni M. Kutchan,Toni M. Kutchan,Toni M. Kutchan +8 more
TL;DR: CYP719B1 therefore is the prototype for a new family of plant cytochromes P450 that catalyze formation of a phenol-couple in opium poppy.
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
Tsuneo Omura,Ryo Sato +1 more
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.
Charles Williams,Henry Kamin +1 more
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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The Carbon Monoxide-binding Pigment of Liver Microsomes II. SOLUBILIZATION, PURIFICATION, AND PROPERTIES
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