Zobrazeno 1 - 10
of 58
pro vyhledávání: '"R. B. Gennis"'
Autor:
A E, Galván, M C, Chalón, L A, Schurig-Briccio, R A, Salomón, C J, Minahk, R B, Gennis, A, Bellomio
Publikováno v:
Biochimica et biophysica acta. Bioenergetics. 1859(2)
Microcin J25 has two targets in sensitive bacteria, the RNA polymerase, and the respiratory chain through inhibition of cellular respiration. In this work, the effect of microcin J25 in E. coli mutants that lack the terminal oxidases cytochrome bd-I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4c7914e455d82c288baf63896d8f6183
https://pubmed.ncbi.nlm.nih.gov/29107655
https://pubmed.ncbi.nlm.nih.gov/29107655
Publikováno v:
Journal of Biological Chemistry. 265:4364-4368
The cytochrome bo quinol oxidase of Escherichia coli is one of two respiratory O2 reductases which the bacterium synthesizes. The enzyme complex contains copper and 2 mol of b-type heme. Electron paramagnetic resonance (epr) spectroscopy of membranes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e0bc9c3aea021bf3c9527cd9b92b7d68
https://doi.org/10.1016/s0021-9258(19)39573-0
https://doi.org/10.1016/s0021-9258(19)39573-0
Publikováno v:
Biochemistry. 34(38)
Cytochrome bd oxidase is a terminal bacterial oxidase containing three cofactors: a low-spin heme (b558), a high-spin heme (b595), and a chlorin d. The center of dioxygen reduction has been proposed to be at a dinuclear b595/d site, whereas b558 is m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d930b6339066486b9dc322909153358
https://pubmed.ncbi.nlm.nih.gov/7547954
https://pubmed.ncbi.nlm.nih.gov/7547954
Publikováno v:
Biokhimiia (Moscow, Russia). 60(2)
The absorption spectrum of the cytochrome bd complex from Escherichia coli in the "as isolated" state is characterized by an intense band at approximately 648 nm belonging to reduced heme d oxycomplex (d2+-O2). This band is often accompanied by a sma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9afd9df715f03bcb30416d4494c261c1
https://pubmed.ncbi.nlm.nih.gov/7718672
https://pubmed.ncbi.nlm.nih.gov/7718672
Publikováno v:
The Journal of biological chemistry. 269(46)
The cytochrome bo3-ubiquinol oxidase, one of two ubiquinol oxidases in Escherichia coli, is a member of the heme-copper oxidase superfamily. The enzyme contains four protein subunits (I-IV) with apparent molecular masses of 58, 33, 22, and 17 kDa, re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::38c25d48b8274c5e01598548fde90916
https://pubmed.ncbi.nlm.nih.gov/7961841
https://pubmed.ncbi.nlm.nih.gov/7961841
Autor:
Tomoko Ohnishi, V. D. Sled', N. I. Rudnitzky, B. W. Jacobson, Y. Fukumori, S. W. Meinhardt, M. W. Calhoun, R. B. Gennis, H. Leif, T. Friedrich, H. Weiss
Publikováno v:
Biochemical Society transactions. 22(1)
The mitochondrial NADH-Q oxidoreductase (Complex I) is the most complex among the major mitochondrial energy coupling enzymes. Complex I from bovine heart and Neurosporu crussu contains 41 (1) and >32 (2) distinct subunits, respectively. In contrast,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d39928a81af430ea8c1a630db952f2c
https://pubmed.ncbi.nlm.nih.gov/8206301
https://pubmed.ncbi.nlm.nih.gov/8206301
Autor:
Terry A. Krulwich, D. B. Hicks, J. C. Rumbley, Peter R. Rich, A. J. Moody, W. J. Ingledew, R. B. Gennis
Publikováno v:
Biochemical Society transactions. 20(3)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62e8db3bbbbbee534cb994fa6ced20d4
https://pubmed.ncbi.nlm.nih.gov/1330766
https://pubmed.ncbi.nlm.nih.gov/1330766
Autor:
R B, Gennis
Publikováno v:
Biochimica et biophysica acta. 1101(2)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::23241ae0da2197c94fb27616da74fa07
https://pubmed.ncbi.nlm.nih.gov/1378758
https://pubmed.ncbi.nlm.nih.gov/1378758
Publikováno v:
The Journal of biological chemistry. 267(9)
The cytochrome b subunit of the bc1 complexes contains two cytochrome components (bL and bH) and is the locus of both a quinol-oxidizing site (Qo or Qz) and a quinone-reducing site (Qi or Qc). Sequence alignments of this subunit from over 20 eukaryot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::862487f1b670f11874b102352574e174
https://pubmed.ncbi.nlm.nih.gov/1313421
https://pubmed.ncbi.nlm.nih.gov/1313421
Publikováno v:
The Journal of biological chemistry. 267(3)
The cytochrome o complex of Escherichia coli is a ubiquinol oxidase which is the predominant respiratory terminal oxidase when the bacteria are grown under high oxygen tension. The amino acid sequences of three of the subunits of this quinol oxidase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7d82e53dc265ba12266c24cb5edb349e
https://pubmed.ncbi.nlm.nih.gov/1309809
https://pubmed.ncbi.nlm.nih.gov/1309809