Proton and electron transfer in bacterial reaction centers.
about
Proton transfer reactions and hydrogen-bond networks in protein environmentsSix-coordinate manganese(3+) in catalysis by yeast manganese superoxide dismutaseStructural insight into the type-II mitochondrial NADH dehydrogenasesMolecular mechanisms for generating transmembrane proton gradientsThermochemistry of proton-coupled electron transfer reagents and its implicationsInvestigating the mechanisms of photosynthetic proteins using continuum electrostaticsFactors influencing the energetics of electron and proton transfers in proteins. What can be learned from calculations.Menaquinone-7 is specific cofactor in tetraheme quinol dehydrogenase CymA.Proton conduction through the M2 protein of the influenza A virus; a quantitative, mechanistic analysis of experimental data.Role of the N- and C-terminal regions of the PufX protein in the structural organization of the photosynthetic core complex of Rhodobacter sphaeroides.Effects of the measuring light on the photochemistry of the bacterial photosynthetic reaction center from Rhodobacter sphaeroides.Residual water modulates QA- -to-QB electron transfer in bacterial reaction centers embedded in trehalose amorphous matrices.Protein engineering of cytochrome b562 for quinone binding and light-induced electron transfer.Hyperfine and nuclear quadrupole tensors of nitrogen donors in the Q(A) site of bacterial reaction centers: correlation of the histidine N(δ) tensors with hydrogen bond strength.Modeling gating charge and voltage changes in response to charge separation in membrane proteinsEvidence from FTIR difference spectroscopy of an extensive network of hydrogen bonds near the oxygen-evolving Mn(4)Ca cluster of photosystem II involving D1-Glu65, D2-Glu312, and D1-Glu329Induced conformational changes upon Cd2+ binding at photosynthetic reaction centersPhotoionization of oxidized coenzyme Q in microemulsion: laser flash photolysis study in biomembrane-like system.RegB kinase activity is controlled in part by monitoring the ratio of oxidized to reduced ubiquinones in the ubiquinone poolMechanisms of proton transfer in proteins: localized charge transfer versus delocalized soliton transferProton-coupled electron flow in protein redox machinesTheory of coupled electron and proton transfer reactions.Proton-coupled electron transfer: the mechanistic underpinning for radical transport and catalysis in biology.Participation of glutamate-354 of the CP43 polypeptide in the ligation of manganese and the binding of substrate water in photosystem IIStigmatellin probes the electrostatic potential in the QB site of the photosynthetic reaction center.Proton coupled electron transfer and redox active tyrosines in Photosystem IIDemonstration of asymmetric electron conduction in pseudosymmetrical photosynthetic reaction centre proteins in an electrical circuitFluorescence relaxation in intact cells of photosynthetic bacteria: donor and acceptor side limitations of reopening of the reaction center.Proton transfer pathways and mechanism in bacterial reaction centers.Affinity and activity of non-native quinones at the Q(B) site of bacterial photosynthetic reaction centers.Time-resolved infrared spectroscopy in the study of photosynthetic systems.Mechanism of proton-coupled quinone reduction in Photosystem II.Hydrogen bonding between the Q(B) site ubisemiquinone and Ser-L223 in the bacterial reaction center: a combined spectroscopic and computational perspective.Photosynthetic diode: electron transport rectification by wetting the quinone cofactor.Redox potential tuning through differential quinone binding in the photosynthetic reaction center of Rhodobacter sphaeroides.Identification of the proton pathway in bacterial reaction centers: both protons associated with reduction of QB to QBH2 share a common entry pointToward theoretical analysis of long-range proton transfer kinetics in biomolecular pumps.Modification of quinone electrochemistry by the proteins in the biological electron transfer chains: examples from photosynthetic reaction centers.Structure-Based Mechanism for Oxidative Decarboxylation Reactions Mediated by Amino Acids and Heme Propionates in Coproheme Decarboxylase (HemQ).Nuclear hyperfine and quadrupole tensor characterization of the nitrogen hydrogen bond donors to the semiquinone of the QB site in bacterial reaction centers: a combined X- and S-band (14,15)N ESEEM and DFT study.
P2860
Q27006718-0C7822EA-236A-48B3-9745-7AD79E647F9BQ27671614-3FDCD6D2-ACC1-4395-9787-BDDD5C7BBBA2Q27682936-C8B36BD3-BDFA-437C-905B-0AD0D9B0AF9BQ28287439-8D6CB3AB-78B0-4896-8396-A75138FCC187Q28744066-5B7B59E3-0056-487A-A00D-0A2772A629DCQ29542853-A22374B0-62DD-45B1-B181-18236ECC8A8CQ30356246-F1C54729-D939-47E8-8C3A-4B9DF2B5E297Q30467920-2FAE9EA9-6B17-484B-A137-110397D61B3CQ30825019-E739A8A1-DFA1-4264-B1A9-81256489B3D0Q30832019-CBFCE26E-FB7C-4452-9A15-084182AE181FQ31024474-D98DCFE9-4157-429B-9890-A7EDA94CFDDDQ33193296-5949FD18-AA9F-4A42-8C27-A4B99FD57F59Q33580348-DFF0CD03-2B00-4547-BBBC-71AE3DE5DE8CQ34020565-FBD4F2CA-D59E-4999-9A1A-8C6ED501F7CDQ34025599-24E9AF91-153C-4F2C-B6F8-867F46197529Q34049865-8D341A16-A6B4-4673-B561-BA3A38FCDB53Q34132176-70666564-897C-43A5-995A-1616A348EEFCQ34279158-093A482B-3E8A-49D0-921E-2958780FBE16Q34398742-CF4EB959-FEC1-407C-8736-4D6D935E712DQ34421563-237C6BD5-994D-413B-9538-A8175ACEBB15Q34423826-105D37D3-237D-4545-929C-FCBD488E34FAQ34423985-C6D524BF-49E5-4209-884D-AE71DA70E699Q34551745-FA7E911D-F60B-43F8-8B89-1A29E4D68C9EQ34951030-9FE96F8D-18B4-4392-BB67-F27CC86D672FQ34996640-94D6974F-2FCD-4CD7-9AAA-7B50F3C3B39AQ35189808-6AEF7419-0880-4787-87FD-668DA7044F90Q35197094-B893A215-3C46-4D6E-9BCC-DAF33995C308Q35531355-32FF9B93-793A-4CE4-812F-9CD27F129D30Q35589966-88F3D098-9B89-4830-ADDB-165B3170E3A3Q35642136-0689833C-F7D6-4F27-93B8-E097C053AEFCQ36146487-0E576CB1-DA2F-4ED8-B4CE-56D7CC02578DQ36545451-824E6B17-0484-4896-AF84-3BEB30E967E1Q36595184-D9DFC33B-5D11-4249-996F-897A8F165F34Q36757281-80329344-E17A-485C-80A4-F08E56F529EAQ37047643-ADCD94D7-1535-4E81-9B01-12D0AB545B5DQ37282071-694E51C4-36A5-45A9-9289-CBC42F609F54Q37309585-83BF21E9-F866-4EE6-A24E-5CE002682AC1Q37315527-CB4F3DD1-17F1-4A01-BA25-8B3EDDB7D29CQ37696971-94FEB884-18A5-461A-961D-7EA03500BAE2Q37697457-C9D7A61A-6DC1-40DF-B6E6-85B3E0FD8FBA
P2860
Proton and electron transfer in bacterial reaction centers.
description
2000 nî lūn-bûn
@nan
2000 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Proton and electron transfer in bacterial reaction centers.
@ast
Proton and electron transfer in bacterial reaction centers.
@en
type
label
Proton and electron transfer in bacterial reaction centers.
@ast
Proton and electron transfer in bacterial reaction centers.
@en
prefLabel
Proton and electron transfer in bacterial reaction centers.
@ast
Proton and electron transfer in bacterial reaction centers.
@en
P2093
P1476
Proton and electron transfer in bacterial reaction centers.
@en
P2093
M L Paddock
M S Graige
M Y Okamura
P304
P356
10.1016/S0005-2728(00)00065-7
P407
P577
2000-05-01T00:00:00Z