Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Christopher W. Higham"'
Publikováno v:
Journal of Biological Chemistry. 278:20500-20506
Cytochrome c maturation in the periplasms of many bacteria requires the heme chaperone CcmE, which binds heme covalently both in vivo and in vitro via a histidine residue before transferring the heme to apocytochromes c. To investigate the mechanism
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e337a8011e6de1e139d23357e423256
https://doi.org/10.1074/jbc.m212925200
https://doi.org/10.1074/jbc.m212925200
Autor:
Janos Hajdu, Christopher W. Higham, Carsten D. Richter, Euan H. J. Gordon, Tove Sjögren, Vilmos Fülöp, James W. A. Allen, Stuart J. Ferguson, Malin Löfqvist
Publikováno v:
Journal of Biological Chemistry. 278:11773-11781
The 1.4-A crystal structure of the oxidized state of a Y25S variant of cytochrome cd(1) nitrite reductase from Paracoccus pantotrophus is described. It shows that loss of Tyr(25), a ligand via its hydroxy group to the iron of the d(1) heme in the oxi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db0d0859de7a381840c57319b0499233
https://doi.org/10.1074/jbc.m211886200
https://doi.org/10.1074/jbc.m211886200
Publikováno v:
Proceedings of the National Academy of Sciences. 99:9703-9708
Three key steps of cytochrome c biogenesis in many Gram-negative bacteria, the uptake of heme by the heme chaperone CcmE, the covalent attachment of heme to CcmE, and its subsequent release from CcmE to an apocytochrome c , have been achieved in vitr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::865a8fe2dc61491f9b48070b11ebbfd3
https://doi.org/10.1073/pnas.152120699
https://doi.org/10.1073/pnas.152120699
Autor:
Nicholas J. Watmough, Christopher W. Higham, Stuart J. Ferguson, Myles R. Cheesman, James W. A. Allen
Publikováno v:
Biochemical and Biophysical Research Communications. 279:674-677
Paracoccus pantotrophus cytochrome cd(1) is a physiological nitrite reductase and an in vitro hydroxylamine reductase. The oxidised "as isolated" form of the enzyme has bis-histidinyl coordinated c-heme and upon reduction its coordination changes to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f476939e9addf3501ab2c3b4bb4bfa7c
https://doi.org/10.1006/bbrc.2000.4009
https://doi.org/10.1006/bbrc.2000.4009
Autor:
Richard S. Zajicek, James W. A. Allen, Nicholas J. Watmough, Christopher W. Higham, Stuart J. Ferguson
The oxidized form of Paracoccus pantotrophus cytochrome cd1 nitrite reductase, as isolated, has bis-histidinyl co-ordination of the c haem and His/Tyr co-ordination of the d1 haem. On reduction, the haem co-ordinations change to His/Met and His/vacan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b7d16d0a11beaee6981a59cbec390ee
https://europepmc.org/articles/PMC1222841/
https://europepmc.org/articles/PMC1222841/
Publikováno v:
FEBS Letters. (1):128-132
The alpha- and beta-anomers of D-cellobiose were resolved by 1H NMR spectroscopy. Addition of cellobiose dehydrogenase purified from the white-rot P. chrysosporium led to selective conversion of beta-D-cellobiose. The product was identical to cellobi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58a3d60d831977033ef31ba37d94d374