Identification of the proton pathway in bacterial reaction centers: decrease of proton transfer rate by mutation of surface histidines at H126 and H128 and chemical rescue by imidazole identifies the initial proton donors.

Identification of the proton pathway in bacterial reaction centers: decrease of proton transfer rate by mutation of surface histidines at H126 and H128 and chemical rescue by imidazole identifies the initial proton donors.

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http://www.wikidata.org/entity/Q43809954
Kinetic analysis of multiple proton shuttles in the active site of human carbonic anhydraseChemical rescue of histidine selectivity filter mutants of the M2 ion channel of influenza A virusInduced conformational changes upon Cd2+ binding at photosynthetic reaction centersProton transfer pathways and mechanism in bacterial reaction centers.Subunit III-depleted cytochrome c oxidase provides insight into the process of proton uptake by proteinsProton control of oxidation and spin state in a series of iron tripodal imidazole complexes.Crystallographic location and mutational analysis of Zn and Cd inhibitory sites and role of lipidic carboxylates in rescuing proton path mutants in cytochrome c oxidase.The two last overviews by Colin Allen Wraight (1945-2014) on energy conversion in photosynthetic bacteria.Multiple scattering x-ray absorption studies of Zn2+ binding sites in bacterial photosynthetic reaction centers.Identification of FTIR bands due to internal water molecules around the quinone binding sites in the reaction center from Rhodobacter sphaeroides.Synthesis and characterization of manganese(II) and iron(III) d5 tripodal imidazole complexes. Effect of oxidation state, protonation state and ligand conformation on coordination number and spin state.The DMPC lipid phase transition influences differently the first and the second electron transfer reactions in bacterial reaction centers.Energetics of proton transfer pathways in reaction centers from Rhodobacter sphaeroides. The Glu-H173 activated mutants.The heme-copper oxidase superfamily shares a Zn2+-binding motif at the entrance to a proton pathway.
P2860

Identification of the proton pathway in bacterial reaction centers: decrease of proton transfer rate by mutation of surface histidines at H126 and H128 and chemical rescue by imidazole identifies the initial proton donors.

Item
http://www.wikidata.org/entity/Q43809954
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh-hant
name
Identification of the proton p ...... ies the initial proton donors.
@en
Identification of the proton p ...... ies the initial proton donors.
@nl
type
label
Identification of the proton p ...... ies the initial proton donors.
@en
Identification of the proton p ...... ies the initial proton donors.
@nl
prefLabel
Identification of the proton p ...... ies the initial proton donors.
@en
Identification of the proton p ...... ies the initial proton donors.
@nl
P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P577
P698
P356
P1433
P1476
Identification of the proton p ...... ies the initial proton donors.
@en
P2093
P304
P31
P356
P407
P433
P478
P577
P698