Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A - Test2 - elhamkhani - TriplyDB

Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A

Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A

http://www.wikidata.org/entity/Q27641819

about

Experimental support for the "E pathway hypothesis" of coupled transmembrane e- and H+ transfer in dihemic quinol:fumarate reductase.Review: studies of ferric heme proteins with highly anisotropic/highly axial low spin (S = 1/2) electron paramagnetic resonance signals with bis-histidine and histidine-methionine axial iron coordination Reversible interconversion of carbon dioxide and formate by an electroactive enzyme Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase Proteins as templates for complex synthetic metalloclusters: towards biologically programmed heterogeneous catalysis Protein Crystallography Reveals a Role for the FS0 Cluster of Escherichia coli Nitrate Reductase A (NarGHI) in Enzyme Maturation Molecular mechanism of energy conservation in polysulfide respiration Structural Basis for the Oxidation of Protein-bound Sulfur by the Sulfur Cycle Molybdohemo-Enzyme Sulfane Dehydrogenase SoxCD Crystal structure of NirD, the small subunit of the nitrite reductase NirbD from Mycobacterium tuberculosis at 2.0 Å resolution A membrane-bound multienzyme, hydrogen-oxidizing, and sulfur-reducing complex from the hyperthermophilic bacterium Aquifex aeolicus Selective selC-independent selenocysteine incorporation into formate dehydrogenases The iron-sulfur clusters in Escherichia coli succinate dehydrogenase direct electron flow Structures of two bacterial resistance factors mediating tRNA-dependent aminoacylation of phosphatidylglycerol with lysine or alanine Nitrate and periplasmic nitrate reductases Hydrogen production by recombinant Escherichia coli strains Biological sources and sinks of nitrous oxide and strategies to mitigate emissions Resolution of distinct membrane-bound enzymes from Enterobacter cloacae SLD1a-1 that are responsible for selective reduction of nitrate and selenate oxyanions Crystal structure of pyrogallol-phloroglucinol transhydroxylase, an Mo enzyme capable of intermolecular hydroxyl transfer between phenols.Optimization of overexpression of a chaperone protein of steroid C25 dehydrogenase for biochemical and biophysical characterization.A respiratory nitrate reductase active exclusively in resting spores of the obligate aerobe Streptomyces coelicolor A3(2).A-type carrier protein ErpA is essential for formation of an active formate-nitrate respiratory pathway in Escherichia coli K-12.The respiratory molybdo-selenoprotein formate dehydrogenases of Escherichia coli have hydrogen: benzyl viologen oxidoreductase activity Evolutionary persistence of the molybdopyranopterin-containing sulfite oxidase protein fold Detecting clusters of mutations Biomimetic chemistry of iron, nickel, molybdenum, and tungsten in sulfur-ligated protein sites.Structures of membrane proteins.Using SAD data in Phaser The molybdenum oxotransferases and related enzymes.Dynamics of the [4Fe-4S] cluster in Pyrococcus furiosus D14C ferredoxin via nuclear resonance vibrational and resonance Raman spectroscopies, force field simulations, and density functional theory calculations.Camelid nanobodies raised against an integral membrane enzyme, nitric oxide reductase The effects of lipids on channel function.Quinol-cytochrome c oxidoreductase and cytochrome c4 mediate electron transfer during selenate respiration in Thauera selenatis.The Qrc membrane complex, related to the alternative complex III, is a menaquinone reductase involved in sulfate respiration.Genomic analysis of anaerobic respiration in the archaeon Halobacterium sp. strain NRC-1: dimethyl sulfoxide and trimethylamine N-oxide as terminal electron acceptors Metabolic engineering to enhance bacterial hydrogen production The mononuclear molybdenum enzymes.A genome-scale metabolic flux model of Escherichia coli K-12 derived from the EcoCyc database.Heme biosynthesis is coupled to electron transport chains for energy generation.Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A.How to make a living from anaerobic ammonium oxidation.

P2860

Q24535858-2EDC8CE8-EBDF-4284-988A-DD0183D531B6 Q24599611-4BCDE26A-6EB9-4DB5-8C9B-E4B1DBB4AC73 Q24652765-0597652F-8D5D-418C-8E1D-806EA71CCACF Q24685587-20B882C5-DDFB-4E8C-B000-8B89F5F53DAC Q26747411-07D1CE47-E08A-4277-A797-5F04E2D85BC5 Q27646632-782D9A33-1015-4429-B022-E876850F8378 Q27650770-FBFA68C1-BD78-4A24-9E73-A8AB69F1790E Q27666328-5FF1F4C9-AECC-4157-BE79-A73A6C93A385 Q27682234-56B24356-CA55-45F1-8830-BF9766C540F5 Q28278010-9FA125E8-E3D2-4D31-A9C4-29FF992BED86 Q28487069-D6BDD3C1-5B7B-4EC3-AF97-9001AD4DF60F Q28492481-A79F520B-B7EB-4C52-B46A-D4EBF69007EE Q28493059-2D140DF2-2123-4043-889E-CF79D847BC4E Q28656337-75F3830F-B012-4484-8E9F-5DE75A507DC4 Q28661846-DF0D8DE8-D941-4480-BC06-6F9BF1CC967D Q28731249-0F86FF3D-A498-483F-9BE0-8A358E893CFF Q28768140-5ABE78E8-FB7C-4D24-88D8-C272A64BFF79 Q30163900-033CEEE5-BBDF-42B8-8A64-F8E6C02088CF Q30252864-9203772B-DEE6-418D-9EAD-84A56714F11C Q30317763-6790D455-1610-45EF-A63C-DE44C7F9C62E Q30318269-20FB9FAD-545E-4FF2-A302-0FB0146D859F Q30318343-F046CF03-06ED-4D79-9AC3-3476ED387682 Q30369786-694CAAB1-BF5D-405E-8540-E71721E22893 Q30373381-46E2D81D-2209-4284-910A-DFFEC594B447 Q30374853-86E11771-34C5-4B8C-99E0-FB9597A7F9D7 Q30391943-ACC42C53-0133-4AD0-B287-321016097F5F Q30401431-3E0B776E-29D7-410F-A143-A58F8B40462A Q30425916-E1953238-3020-4FA5-A47C-3491BE3BC993 Q30466601-7A674EAF-7816-4D9F-AA39-98171C0386CF Q33412211-6BD663E4-8190-4D09-8015-ED6E58B76394 Q33509655-83C2AE1D-EB33-4A74-9ACC-66E4BA792C94 Q33554128-A5C1DE96-A9FA-40BD-A9B6-468866AF56D3 Q33586014-EDAC3F59-2507-43A4-81C9-812C4EC653AB Q33714526-FD8AF176-AE0F-4954-9C22-0256194AAF5E Q33801562-BF74CE6D-77C7-4244-812E-21E0E753DC3C Q33840734-B818CEE6-904C-4DE3-8A9C-B33272015F8A Q33863113-63F0208D-8422-48D5-B4ED-1F582D5EA844 Q33935157-7A417995-12AD-4705-98A4-15C4C25424B7 Q33983981-67C70609-59B9-45DF-8B1A-B831921D9DA5 Q34034634-74E1F7AD-63E4-40F2-AE22-FEADB50B67E6

P2860

Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A

http://www.wikidata.org/entity/Q27641819

description

2003 nî lūn-bûn

@nan

2003 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2003年の論文

@ja

2003年論文

@yue

2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

name

Insights into the respiratory ...... ructure of nitrate reductase A

@ast

Insights into the respiratory ...... ructure of nitrate reductase A

@en

Insights into the respiratory ...... ructure of nitrate reductase A

@nl

type

label

Insights into the respiratory ...... ructure of nitrate reductase A

@ast

Insights into the respiratory ...... ructure of nitrate reductase A

@en

Insights into the respiratory ...... ructure of nitrate reductase A

@nl

prefLabel

Insights into the respiratory ...... ructure of nitrate reductase A

@ast

Insights into the respiratory ...... ructure of nitrate reductase A

@en

Insights into the respiratory ...... ructure of nitrate reductase A

@nl

P1433

Q27641819-CB70DECD-F635-4375-972B-D5F6E88D935E

P1476

Q27641819-6C1FA468-8387-445A-820C-C0C2340B1B30

P2093

Q27641819-2C08711E-646C-4FA7-B44C-DBF8503AE858

Q27641819-2CF33FD0-0799-42CE-9040-A96AC118829E

Q27641819-2E06A4E3-7009-4E1F-BEC6-91312FE07413

Q27641819-34E40985-0517-4112-B1FC-E7593D4FA440

Q27641819-57730B42-3703-40DA-9AEE-F3D2E5B18EDF

Q27641819-9F41E0AA-B51C-4140-BFA9-07DCA6DE72D6

Q27641819-C46C84F3-CB3C-4250-AE87-A3E40B3E1B45

Q27641819-EE8822C6-4BD8-4FE8-BE38-FEB16F284F7C

P2860

Q27641819-00E2CA2A-382C-4603-8EC8-DA328E808002

Q27641819-146A3344-7ECC-43AA-AD33-887E8BADE30A

Q27641819-195B42FB-7EBB-403E-A764-7F6852813A8E

Q27641819-1AEE6DEA-1E60-498F-A21B-ECAC0B777D39

Q27641819-1B9A50D2-D9C8-4F17-ADE8-8BC23C86B723

Q27641819-27E531F3-5C61-4527-B585-EC6934C12FE3

Q27641819-2B6EE850-BD0B-48C8-AD2C-577E3183533B

Q27641819-2C124D5C-A621-40EE-AF08-23E2B084A831

Q27641819-2C3C5CE7-A3FF-4447-9EF6-C41D45F26C29

Q27641819-2C402A67-3167-4076-8325-0D6491138A3B

P2888

Q27641819-8858EE43-929F-4E7E-9344-386C47890D05

P304

Q27641819-29CAAECF-E654-4291-B062-97E686C90428

P31

Q27641819-E53830C3-2769-4A3E-9152-0AEB058C370A

P3181

Q27641819-1D66CCDC-00A9-471F-A496-F283FF66E051

P356

Q27641819-3F991BEE-AE20-43BB-9C6C-95A919286642

P407

Q27641819-653E9CE6-C9F2-4138-A44F-D4BF65E5C9B3

P433

Q27641819-A6107031-D649-43BE-91BE-8399E72C1C9F

P478

Q27641819-77B6C288-7AB8-45D9-9B39-3E1EDFA05214

P577

Q27641819-DE3442B3-59A4-442A-82D8-0C5C5ACBCC4F

P5875

Q27641819-6DFD038A-D24C-4FE5-9E61-A06A29A055EC

P6179

Q27641819-37CE7A6C-BDA0-4EC0-9A3A-663FB46A5A4D

P698

Q27641819-FFCB06B1-7035-4F04-9380-75EECD57A831

P921

Q27641819-1A492CF1-EA9D-4DE8-A8CB-8C557EE75962

Q27641819-CFC629A1-FBA9-4CEF-AD1B-AAA07E35F7B4

Q27641819-E5567A14-7B0C-4916-8F76-F6F4E49F1146

P3181

P356

P1433

Nature structural biology

P1476

Insights into the respiratory ...... ructure of nitrate reductase A

@en

P2093

Cynthia Hou

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

Daniel Lim

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

Francis Blasco

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

Joel H Weiner

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

Michela G Bertero

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

Monica Palak

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

Natalie C J Strynadka

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

Richard A Rothery

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

P2860

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Processing of X-ray diffraction data collected in oscillation mode

Crystal structure of the first dissimilatory nitrate reductase at 1.9 A solved by MAD methods

Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution

Molecular basis of proton motive force generation: structure of formate dehydrogenase-N

Architecture of succinate dehydrogenase and reactive oxygen species generation

Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas

Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 A resolution

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

P2888

P304

681-7

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

P31

scholarly article

P3181

1931367

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

P356

10.1038/NSB969

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

P407

P433

9

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

P478

10

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

P577

2003-09-01T00:00:00Z

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

P5875

10620539

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

P6179

1050182424

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

P698

12910261

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

P921

molybdenum incorporation via L-aspartyl molybdenum bis(molybdopterin guanine dinucleotide)

nitrate reductase activity involved in anaerobic electron transport chain