Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Matthew G. Goodwin"'
Publikováno v:
FEBS Letters. 540:234-240
Photo-excitation of membrane-bound Rhodobacter sphaeroides reaction centres containing the mutation Ala M260 to Trp (AM260W) resulted in the accumulation of a radical pair state involving the photo-oxidised primary electron donor (P). This state had
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6cb31ae7fe70c9df98938c7556123671
https://doi.org/10.1016/s0014-5793(03)00270-9
https://doi.org/10.1016/s0014-5793(03)00270-9
Publikováno v:
Microbiology. 147:2493-2504
The complete genome sequence of Helicobacter pylori has revealed the presence of a novel set of chemotaxis genes including three cheV paralogues. CheV is a bi-functional protein, the N-terminal domain being homologous to the signalling-complex linker
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca80ab2e288d09c5a56d3f3382509204
https://doi.org/10.1099/00221287-147-9-2493
https://doi.org/10.1099/00221287-147-9-2493
Publikováno v:
Photosynthesis Research. 59:9-26
Three single-site mutations have been introduced at positions close to the QA ubiquinone in the reaction centre from Rhodobacter sphaeroides. Two of these mutations, Ala M260 to Trp and Ala M248 to Trp, result in a reaction centre that does not suppo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::10500379ba8ae2db41534d1dee5c105c
https://doi.org/10.1023/a:1006111321083
https://doi.org/10.1023/a:1006111321083
Publikováno v:
Biochemical Society Transactions. 26:422-427
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::073a3b8162a0d5e9e3a5b4d3028541a6
https://doi.org/10.1042/bst0260422
https://doi.org/10.1042/bst0260422
Publikováno v:
Biochemical Journal. 319:839-842
The reconstitution of active holoenzyme containing calcium from inactive calcium-free methanol dehydrogenase, isolated from a moxA mutant of Methylobacterium extorquens, has a pH optimum of about pH 10, with a well defined pK for the process at pH 9.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::acdf51797748cacfd85878d885dbda78
https://doi.org/10.1042/bj3190839
https://doi.org/10.1042/bj3190839
Publikováno v:
Biochemical Journal. 307:735-741
All cysteines in methanol dehydrogenase (MDH) from Methylobacterium extorquens are involved in intra-subunit disulphide bridge formation. One of these is between adjacent cysteine residues which form a novel ring structure in the active site. It is r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1917631e4d9b86777218491d7afbbddc
https://doi.org/10.1042/bj3070735
https://doi.org/10.1042/bj3070735
Publikováno v:
Structure. 3(2):177-187
Background: Methanol dehydrogenase (MDH) is a bacterial periplasmic quinoprotein; it has pyrrolo-quinoline quinone (PQQ) as its prosthetic group, requires Ca 2+ for activity and uses cytochrome c L as its electron acceptor. Low-resolution structures
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c766b7d6209bb167be5941c8a73e13b7
Autor:
Matthew G. Goodwin, Marion E. van Brederode, Rienk van Grondelle, Michael R. Jones, Justin P. Ridge
Publikováno v:
Biochemical Society transactions. 26(3)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcf92f242952a6c8d47f5b0f5a033629
https://pubmed.ncbi.nlm.nih.gov/9765928
https://pubmed.ncbi.nlm.nih.gov/9765928
Autor:
Matthew G Goodwin, Christopher Anthony
Publikováno v:
The Biochemical journal. 318
The quinoprotein methanol dehydrogenase (MDH) contains a Ca2+ ion at the active site. Ca(2-)-free enzyme (from a processing mutant) was used to obtain enzyme containing Sr2+ or Ba2+, the Ba(2+)-MDH being the first enzyme to be described in which a Ba
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::405858f6f75de0e26d5021dd2ee6cf69
https://pubmed.ncbi.nlm.nih.gov/8809062
https://pubmed.ncbi.nlm.nih.gov/8809062
Autor:
Matthew G. Goodwin, J. Baz Jackson
Publikováno v:
Biochimica et biophysica acta. 1144(2)
Light-Harvesting Complexes I and II (LHI and LHII) were extracted from chromatophores of Rhodobacter capsulatus, purified in Triton X-100 and reconstituted into phospholipid vesicles. Application of membrane potentials (K+ diffusion potentials) to LH
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45b13cf00a0e8f414563b43bd328a64f
https://pubmed.ncbi.nlm.nih.gov/8369337
https://pubmed.ncbi.nlm.nih.gov/8369337