Expanding the substrates for a bacterial hydrogenlyase reaction. - Wikidata - wikimedia - TriplyDB

Expanding the substrates for a bacterial hydrogenlyase reaction.

Expanding the substrates for a bacterial hydrogenlyase reaction.

http://www.wikidata.org/entity/Q30313185

about

The Ferredoxin-Like Proteins HydN and YsaA Enhance Redox Dye-Linked Activity of the Formate Dehydrogenase H Component of the Formate Hydrogenlyase Complex.Hydrogen production by Sulfurospirillum species enables syntrophic interactions of Epsilonproteobacteria

P2860

Q55426809-38B1C6CB-6587-400F-9B8B-3274B86FA25A Q59125224-7053A892-5215-4247-A5A5-D69CD6B47BA6

P2860

Expanding the substrates for a bacterial hydrogenlyase reaction.

http://www.wikidata.org/entity/Q30313185

description

2017 nî lūn-bûn

@nan

2017 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2017 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2017年の論文

@ja

2017年論文

@yue

2017年論文

@zh-hant

2017年論文

@zh-hk

2017年論文

@zh-mo

2017年論文

@zh-tw

2017年论文

@wuu

name

Expanding the substrates for a bacterial hydrogenlyase reaction.

@ast

Expanding the substrates for a bacterial hydrogenlyase reaction.

@en

type

label

Expanding the substrates for a bacterial hydrogenlyase reaction.

@ast

Expanding the substrates for a bacterial hydrogenlyase reaction.

@en

prefLabel

Expanding the substrates for a bacterial hydrogenlyase reaction.

@ast

Expanding the substrates for a bacterial hydrogenlyase reaction.

@en

P1433

Q30313185-AD2FC25B-9084-45D6-93D6-39434DB6FBFA

P1476

Q30313185-EF84F9CE-0A87-49B8-9F07-79956CF4BD0F

P2093

Q30313185-05F80AE9-586B-427E-A6A6-A01330EFB75B

Q30313185-A917B5E4-56D6-4F2C-B48A-1787C088A672

Q30313185-ADE272CF-6CAA-4175-ABA5-581D920EED46

P2860

Q30313185-26017F4B-F2CF-445A-BF1F-68791A8FFD88

Q30313185-44089CE4-2038-46A7-983A-8FECC9F280E6

Q30313185-442834BB-31D5-4D70-9310-11962EF52CB2

Q30313185-4E81FBA8-CA7E-4468-8233-5F755F36F064

Q30313185-51CF0A06-1558-4D35-844E-791B256E39C7

Q30313185-56809152-DC15-46AF-AB7A-379ECF88B804

Q30313185-569D6A6D-12F6-4DC0-806D-8AC6CA328790

Q30313185-5CE30618-4441-4D42-98AD-F1DD75EE4D50

Q30313185-6D6C29A5-BCAF-461E-8F1D-2EFECCB7F389

Q30313185-70801711-374E-444E-B401-2A2A5F86211D

P304

Q30313185-CFA9E54D-26DF-434B-9CC9-8991D1975F5D

P31

Q30313185-82541A69-3239-4125-A98D-0B756A17EA24

P356

Q30313185-A7C7D3A7-73DA-452D-BAAD-C93EE81F4CB2

P433

Q30313185-6C197450-F0A3-4225-9DA2-3B0854720118

P478

Q30313185-B5DC6A8F-71C7-46BD-B19A-3F9B65EB1A94

P50

Q30313185-0C63810D-DAD2-4E80-9EE3-1E2EEDA9C5C0

Q30313185-23F85988-D7AB-410C-A6E4-8694D939FDCA

Q30313185-CC548EEE-7E10-4D1C-AD25-EBA424716736

P577

Q30313185-45882785-7E7F-4148-81D7-43CE80CEB93D

P698

Q30313185-485B526B-B147-486F-B9F1-C5DA54D9D9C8

P932

Q30313185-497657CB-F74D-4FD9-A9FB-CD0386DC5B3A

P356

P1433

P1476

Expanding the substrates for a bacterial hydrogenlyase reaction.

@en

P2093

Ciaran M Lamont

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

Frank Sargent

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

Grant Buchanan

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

P2860

Energy conservation in chemotrophic anaerobic bacteria

Pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus, functions as a CoA-dependent pyruvate decarboxylase

The dual effect of a ferredoxin-hydrogenase fusion protein in vivo: successful divergence of the photosynthetic electron flux towards hydrogen production and elevated oxygen tolerance

Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster

The complete genome sequence of Escherichia coli K-12

Bacterial formate hydrogenlyase complex

Intact Functional Fourteen-subunit Respiratory Membrane-bound [NiFe]-Hydrogenase Complex of the Hyperthermophilic ArchaeonPyrococcus furiosus

Physiology and bioenergetics of [NiFe]-hydrogenase 2-catalyzed H2-consuming and H2-producing reactions in Escherichia coli.

PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin.

Lactose genes fused to exogenous promoters in one step using a Mu-lac bacteriophage: in vivo probe for transcriptional control sequences.

P304

649-653

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

P31

scholarly article

P356

10.1099/MIC.0.000471

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

P433

5

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

P478

163

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

P50

Constanze Pinske

Ciarán L Kelly

P577

2017-05-10T00:00:00Z

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

P698

28488566

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

P932

5817251

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