Zobrazeno 1 - 10
of 37
pro vyhledávání: '"W J Ingledew"'
Autor:
W. J. Ingledew, Peter R. Rich
Publikováno v:
Biochemical Society Transactions. 33:886-889
Vibrational changes in the catalytic site of horseradish peroxidase were investigated by FTIR (Fourier-transform infrared) spectroscopy in the 1000–2500 cm−1 range. Difference spectra were generated by photolysis of the haemII-CO compound at diff
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3452a577628fb380d2fd8e3eb55d558
https://doi.org/10.1042/bst0330886
https://doi.org/10.1042/bst0330886
Publikováno v:
European Journal of Biochemistry. 255:317-323
The quinol oxidase, cytochrome bd, functions as a terminal oxidase in the Escherichia coli respiratory chain, reducing O2 to water and using ubiquinol-8 or menaquinol-8 as its immediate reductant. The oxidation of quinol is by the low-spin ferri-haem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8843e676ecf26202c232a00722ca6db5
https://doi.org/10.1046/j.1432-1327.1998.2550317.x
https://doi.org/10.1046/j.1432-1327.1998.2550317.x
Publikováno v:
Biochemistry. 35:6345-6350
Flavocytochrome b2 from Saccharomyces cerevisiae couples L-lactate dehydrogenation to cytochrome c reduction in the mitochondrial intermembrane space. The catalytic cycle for this process can be described in terms of five consecutive electron-transfe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3a7e15d7a2277a85d2ec6a4328eb80b
https://doi.org/10.1021/bi9522559
https://doi.org/10.1021/bi9522559
Publikováno v:
Biochemistry. 32:11524-11529
The bo-type ubiquinol oxidase of Escherichia coli is a member of the superfamily of structurally related heme-copper respiratory oxidases. The members of this family, which also includes the aa3-type cytochrome c oxidases, contain at least two heme p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8645ebc7657406dfc01dfe11470c21a0
https://doi.org/10.1021/bi00094a008
https://doi.org/10.1021/bi00094a008
Publikováno v:
Biochemical Journal. 282:255-259
The Escherichia coli cytochrome bd complex incorporates three haems as prosthetic groups. In the ferric form these are a predominantly high-spin chlorin (haem d), a high-spin haem b (b595) and a low-spin haem b (b558). The orientations of these three
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6173169a0e3a511d9f2267d25cdbf89e
https://doi.org/10.1042/bj2820255
https://doi.org/10.1042/bj2820255
Publikováno v:
Journal of Biological Chemistry. 267:2105-2113
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=doi_________::7888cd477a94d00dbcd64ad0e657bd42
https://doi.org/10.1016/s0021-9258(18)46058-9
https://doi.org/10.1016/s0021-9258(18)46058-9
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. 41(26)
Improvements in sensitivity and data processing of Fourier transform infrared (FTIR) spectroscopy enable it to be used to detect changes in protein structure at the atomic level. This paper reports a study of neuronal nitric oxide synthase (nNOS) by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e21bb4176ee9058c1c88c3fca0d52268
https://pubmed.ncbi.nlm.nih.gov/12081486
https://pubmed.ncbi.nlm.nih.gov/12081486
Publikováno v:
European journal of biochemistry. 267(17)
The putative oxidation of ubiquinol by the cytochrome bo3 terminal oxidase of Escherichia coli in sequential one-electron steps requires stabilization of the semiquinone. ENDOR spectroscopy has recently been used to study the native ubisemiquinone ra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::89985a40bcc19c50e61db9579f88f5a1
https://pubmed.ncbi.nlm.nih.gov/10951225
https://pubmed.ncbi.nlm.nih.gov/10951225