Mapping solvation dynamics at the function site of flavodoxin in three redox states - Wikidata - awgldk - TriplyDB

Mapping solvation dynamics at the function site of flavodoxin in three redox states

Mapping solvation dynamics at the function site of flavodoxin in three redox states

http://www.wikidata.org/entity/Q34145264

about

Dynamics and mechanisms of DNA repair by photolyase NADPH-cytochrome P450 oxidoreductase: prototypic member of the diflavin reductase family.Picosecond-resolved fluorescent probes at functionally distinct tryptophans within a thermophilic alcohol dehydrogenase: relationship of temperature-dependent changes in fluorescence to catalysis.Role of a Conserved Tyrosine Residue in the FMN-Heme Interdomain Electron Transfer in Inducible Nitric Oxide Synthase.Picosecond-resolved fluorescence studies of substrate and cofactor-binding domain mutants in a thermophilic alcohol dehydrogenase uncover an extended network of communication.Reconciling mediating and slaving roles of water in protein conformational dynamics.Electron tunneling pathways and role of adenine in repair of cyclobutane pyrimidine dimer by DNA photolyase.Ultrafast dynamics of nonequilibrium electron transfer in photoinduced redox cycle: solvent mediation and conformation flexibility Femtosecond conical intersection dynamics of tryptophan in proteins and validation of slowdown of hydration layer dynamics Validation of response function construction and probing heterogeneous protein hydration by intrinsic tryptophan Ultrafast real-time visualization of active site flexibility of flavoenzyme thymidylate synthase ThyX Mutants of Cytochrome P450 Reductase Lacking Either Gly-141 or Gly-143 Destabilize Its FMN Semiquinone Determining complete electron flow in the cofactor photoreduction of oxidized photolyase Direct probing of solvent accessibility and mobility at the binding interface of polymerase (Dpo4)-DNA complex.Femtosecond dynamics of short-range protein electron transfer in flavodoxin Dynamic Determination of Active-Site Reactivity in Semiquinone Photolyase by the Cofactor Photoreduction Direct examination of the relevance for folding, binding and electron transfer of a conserved protein folding intermediate.Ultrafast 2D-IR spectroelectrochemistry of flavin mononucleotide.Effect of ionic liquid on the native and denatured state of a protein covalently attached to a probe: solvation dynamics study.

P2860

Q28081845-B35FBF33-DD87-4D26-BA5D-2D6C14FD9A1A Q30537968-28856491-663F-4A32-95D3-1A2355CBC74C Q33752775-ABC89CE1-9AF6-4A7E-8887-090E89CAFDAD Q33926497-9418B35C-6E17-4101-925B-9E599D456965 Q34408218-8DAD3925-E8DE-48A3-8598-72CA3709FDCE Q34673378-8CBC05B3-B7CA-4B4F-B907-4A12517DC04E Q35965630-B1B99F23-B21F-4A04-9BA6-1775BAAC2A05 Q36137588-DB7F647A-463F-4FF7-967E-CF34E6FDC48A Q36309852-5E419D4D-E0E8-4B89-B020-E95E5C040657 Q36403624-E814B36C-3BF5-4108-A6E9-3F552B7FB857 Q36895631-40915E1A-30F0-41C8-AEC6-59A07F496F69 Q37078680-F08FBDE2-9E17-4AC8-AEDE-D90D390D65D8 Q37088695-84085EE2-3B3B-4D8E-8E71-36F1E501D704 Q37521665-49F15EC3-01AE-4F59-AE21-4FDE722E47B0 Q37539929-5C5A18D4-19C4-49A7-9F51-AE080C26BF8B Q37701688-918DD3EB-0465-4F0F-A76E-286455AFE519 Q38681724-94CE658C-67B0-45D4-B28A-2A15CB75BE24 Q40863158-DF93A5DF-86F0-4DB0-87A5-BE1B7ACAE4BF Q50505226-7E8300A1-956D-4C75-B8CE-13F2F95403E7

P2860

Mapping solvation dynamics at the function site of flavodoxin in three redox states

http://www.wikidata.org/entity/Q34145264

description

2010 nî lūn-bûn

@nan

2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Mapping solvation dynamics at the function site of flavodoxin in three redox states

@ast

Mapping solvation dynamics at the function site of flavodoxin in three redox states

@en

Mapping solvation dynamics at the function site of flavodoxin in three redox states

@nl

type

label

Mapping solvation dynamics at the function site of flavodoxin in three redox states

@ast

Mapping solvation dynamics at the function site of flavodoxin in three redox states

@en

Mapping solvation dynamics at the function site of flavodoxin in three redox states

@nl

prefLabel

Mapping solvation dynamics at the function site of flavodoxin in three redox states

@ast

Mapping solvation dynamics at the function site of flavodoxin in three redox states

@en

Mapping solvation dynamics at the function site of flavodoxin in three redox states

@nl

P1433

Q34145264-74EF86F6-9CC6-4EC6-8E40-01C93DD31973

P1476

Q34145264-50ECC11B-DA79-498B-ADEC-B088336277CC

P2093

Q34145264-42C1010F-B261-41F1-9949-246FE85A843D

Q34145264-4DB2A770-5182-496B-9E6D-BEC3DAFB00EB

Q34145264-6CDD0203-6989-4A13-8799-B07C82973AD3

Q34145264-BBED0835-6D61-4BCA-AD5F-ED417B1A2C29

Q34145264-D17469B4-8E3E-4E84-9A19-A4E221EC4FBF

Q34145264-EE40461A-37E8-4456-B24E-FB952A30088D

Q34145264-EEE8407D-B64E-42DF-9003-081EA5B16D14

P2860

Q34145264-13C81F2D-6584-467D-8B16-585F13C9EB1A

Q34145264-29718263-BA85-4833-A47A-E09FDDB52A35

Q34145264-331F8306-D9EC-408C-9D22-2A47B822E23F

Q34145264-33462551-8804-4161-B995-A4158570D1A5

Q34145264-353830DF-F71F-4261-BB7B-8EA6D04CFEB2

Q34145264-3C9B3EC1-3400-4B46-965A-080EBC8A70DA

Q34145264-3CEB1297-EC3C-4698-8FBB-A3E69F9EECFC

Q34145264-3EC53183-9743-422D-9674-49FA5E3F1CDE

Q34145264-471FD0C9-3C4E-4A00-8D48-611859F1B922

Q34145264-4A24FF2A-DB30-4D08-9E0A-D4A4FD78A203

P304

Q34145264-C9557380-EAC8-413E-B183-196B8D0F0E10

P31

Q34145264-92506CD8-2469-4844-A5E1-BF0E5E255689

P356

Q34145264-F6D76A66-44A9-4620-A300-F2701E34A146

P407

Q34145264-B5D9D754-EBB1-4B31-8618-491272E0C460

P433

Q34145264-F69A64BF-768F-4563-8A80-09C1FAB66799

P478

Q34145264-E15DE402-DC7D-4EB7-8F4C-A183953C62A8

P577

Q34145264-BE18C6DD-239C-4350-A26F-27AED2561E6E

P5875

Q34145264-241F30F2-E03F-45E1-9CDE-B6FC43E10DB5

P698

Q34145264-975D2E11-4B40-410B-B6A8-E686279A6D30

P932

Q34145264-5ED2900A-1C38-4B9E-BE8E-F304908E7D6B

P356

P1433

Journal of the American Chemical Society

P1476

Mapping solvation dynamics at the function site of flavodoxin in three redox states

@en

P2093

Chih-Wei Chang

http://www.w3.org/2001/XMLSchema#string

Dongping Zhong

http://www.w3.org/2001/XMLSchema#string

Jeffrey A Stevens

http://www.w3.org/2001/XMLSchema#string

Lijuan Wang

http://www.w3.org/2001/XMLSchema#string

Lijun Guo

http://www.w3.org/2001/XMLSchema#string

Tanping Li

http://www.w3.org/2001/XMLSchema#string

Ting-Fang He

http://www.w3.org/2001/XMLSchema#string

P2860

Flavodoxin: a compromise between efficiency and versatility in the electron transfer from Photosystem I to Ferredoxin-NADP(+) reductase

Comparison of the crystal structures of a flavodoxin in its three oxidation states at cryogenic temperatures

Closure of a tyrosine/tryptophan aromatic gate leads to a compact fold in apo flavodoxin

The chemical and biological versatility of riboflavin

Structure and function of DNA photolyase and cryptochrome blue-light photoreceptors

Protein surface hydration mapped by site-specific mutations.

Cryptochromes: blue light receptors for plants and animals.

Ultrafast solvation dynamics at binding and active sites of photolyases

Spectral tuning in photoactive yellow protein by modulation of the shape of the excited state energy surface

Flavoenzymes: diverse catalysts with recurrent features.

P304

12741-12747

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1021/JA1050154

http://www.w3.org/2001/XMLSchema#string

P407

P433

36

http://www.w3.org/2001/XMLSchema#string

P478

132

http://www.w3.org/2001/XMLSchema#string

P577

2010-09-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

45819521

http://www.w3.org/2001/XMLSchema#string

P698

20731381

http://www.w3.org/2001/XMLSchema#string

P932

2943414

http://www.w3.org/2001/XMLSchema#string