Roles of glutamates and metal ions in a rationally designed nitric oxide reductase based on myoglobin - Wikidata - awgldk - TriplyDB

Roles of glutamates and metal ions in a rationally designed nitric oxide reductase based on myoglobin

Roles of glutamates and metal ions in a rationally designed nitric oxide reductase based on myoglobin

http://www.wikidata.org/entity/Q27660923

about

Beyond directed evolution--semi-rational protein engineering and design Protein design: toward functional metalloenzymes Introducing a 2-His-1-Glu Nonheme Iron Center into Myoglobin Confers Nitric Oxide Reductase Activity Structural basis of biological N2O generation by bacterial nitric oxide reductase Azurin as a Protein Scaffold for a Low-coordinate Nonheme Iron Site with a Small-molecule Binding Pocket Crystal structure of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus Spectroscopic and Computational Study of a Nonheme Iron Nitrosyl Center in a Biosynthetic Model of Nitric Oxide Reductase Rational design of heterodimeric protein using domain swapping for myoglobin Enhancing Mn(II)-Binding and Manganese Peroxidase Activity in a Designed Cytochrome c Peroxidase through Fine-Tuning Secondary-Sphere Interactions Distinct roles of a tyrosine-associated hydrogen-bond network in fine-tuning the structure and function of heme proteins: two cases designed for myoglobin Characterization of the nitric oxide reductase from Thermus thermophilus.Structural analysis of heme proteins: implications for design and prediction.Bioinspired heme, heme/nonheme diiron, heme/copper, and inorganic NOx chemistry: *NO((g)) oxidation, peroxynitrite-metal chemistry, and *NO((g)) reductive coupling.Spectroscopic characterization of mononitrosyl complexes in heme--nonheme diiron centers within the myoglobin scaffold (Fe(B)Mbs): relevance to denitrifying NO reductase Highly diastereoselective and enantioselective olefin cyclopropanation using engineered myoglobin-based catalysts.Intermolecular carbene S-H insertion catalysed by engineered myoglobin-based catalysts†.Computational strategies for the design of new enzymatic functions A biosynthetic model of cytochrome c oxidase as an electrocatalyst for oxygen reduction.Recent advances in biosynthetic modeling of nitric oxide reductases and insights gained from nuclear resonance vibrational and other spectroscopic studies.Spectroscopic and Crystallographic Evidence for the Role of a Water-Containing H-Bond Network in Oxidase Activity of an Engineered Myoglobin.Efficient conversion of primary azides to aldehydes catalyzed by active site variants of myoglobin Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics.Myoglobin-Catalyzed Olefination of Aldehydes Biotinylated Rh(III) complexes in engineered streptavidin for accelerated asymmetric C-H activation Design of Heteronuclear Metalloenzymes.The production of nitrous oxide by the heme/nonheme diiron center of engineered myoglobins (Fe(B)Mbs) proceeds through a trans-iron-nitrosyl dimer.Crystal structures of nitric oxide reductases provide key insights into functional conversion of respiratory enzymes.Rational heme protein design: all roads lead to Rome.Metalloenzyme design and engineering through strategic modifications of native protein scaffolds.Recent advances in rational approaches for enzyme engineering.Why copper is preferred over iron for oxygen activation and reduction in haem-copper oxidases.Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities.Design and engineering of artificial oxygen-activating metalloenzymes.Effect of Outer-Sphere Side Chain Substitutions on the Fate of the trans Iron-Nitrosyl Dimer in Heme/Nonheme Engineered Myoglobins (Fe(B)Mbs): Insights into the Mechanism of Denitrifying NO Reductases Protein evolution analysis of S-hydroxynitrile lyase by complete sequence design utilizing the INTMSAlign software.Manganese and Cobalt in the Nonheme-Metal-Binding Site of a Biosynthetic Model of Heme-Copper Oxidase Superfamily Confer Oxidase Activity through Redox-Inactive Mechanism.Conversion of Nitric Oxide into Nitrous Oxide as Triggered by the Polarization of Coordinated NO by Hydrogen Bonding.Site-specific covalent attachment of heme proteins on self-assembled monolayers.Effect of distal histidines on hydrogen peroxide activation by manganese reconstituted myoglobin.Interactions of uranyl ion with cytochrome b₅ and its His39Ser variant as revealed by molecular simulation in combination with experimental methods.

P2860

Q24604225-2247342B-D70B-4DB4-A68D-5965835F1535 Q26866201-33548F2F-E055-46DF-84E9-26019FD0FF77 Q27662875-B29F16BC-560A-4DB8-9835-475D604054CE Q27666067-71150DFC-011C-4803-948B-3BAEF8619C06 Q27675182-C62D0B91-9F07-4598-AFF1-C6F949869FC2 Q27676836-4E0004AD-F23E-4EBD-B12B-860C6F39959E Q27681543-91E36F2A-14E5-4F75-A384-D1BE78FCA714 Q27696139-27A23E5B-90E0-4EB1-8F27-567B5BB60EC5 Q27704037-2D6F9783-51EA-427A-993A-BB0D0B82267C Q27723238-EEE54256-ABB2-487A-B75A-A2DB0BDACFDA Q30655490-CBD9A3D2-053B-47FF-8099-C140FF39B154 Q33836331-1C61EB59-0881-45BB-B5EE-2C03B9ED90A9 Q34062209-6882A118-6B6D-423B-BFF2-38AFA93E6FFE Q35074627-D43A5835-2FAF-4EDB-8F23-80E6C64A6E3D Q35751495-177C98DB-E356-47C8-B68D-FF90D86DFC58 Q35761129-91EE5582-3B25-4966-9E56-9C31080D01BD Q36011420-A7F1638D-ABFB-4A50-B4AB-30BF68EC828A Q36249818-4B2C0ADF-88E2-4DC1-925D-C241844A68AB Q36368019-FFF9B14B-876C-4BFE-975E-5024C9E36B8D Q36571170-D0AC96B8-CA35-4AE5-901C-92C7BC79E44B Q36584087-E219AB3B-8E83-4CE0-9E3B-0D32BD1E4F64 Q36601149-75153D45-0CA8-4E17-8F68-554ECC8361D2 Q36699296-2637C2A5-2F2A-47AB-80E1-91FA6CA8F08F Q37286557-610A15D4-203E-4667-A209-0CB022512EB5 Q37503700-D79D2CC6-DD23-4E71-8560-8F6810EF259F Q37731552-25808CCC-DFDA-4E4D-8B1F-8645F0068490 Q38078889-D3BB263A-BF3C-4D7E-B593-45401CE8D43A Q38109124-A8AA7867-E8CA-469A-A707-2FF82D65546A Q38186931-ED91B128-EA36-49AE-A0E9-4BFE80F1DB62 Q38201023-321CE84A-280F-4245-BC1B-0BFFE5EA1164 Q38755013-EEF43901-6E50-47DE-A655-D311D5BD107C Q38780554-276AD129-1389-470E-B0FE-B29679E9AB99 Q38876136-F279D805-466F-42D3-82D2-A0917ABAE227 Q39775133-5F8D6DCC-A776-43E3-B21E-DA38C4713F45 Q42624383-6D1F3C00-B508-4CE3-90B7-9E9B8080F4B0 Q46327151-6A000DF5-5747-4409-B0B2-355D127A1B4D Q46575749-0D5A16E4-F700-404E-823C-DF58161A9632 Q47421752-4D56374B-E5B6-4B8D-A2D4-EAA8D29399C5 Q51075700-7D526369-4AF8-4854-94DF-E9A1A91193B9 Q52612278-2916ACBD-3BE6-4460-B915-9757800ACA4B

P2860

Roles of glutamates and metal ions in a rationally designed nitric oxide reductase based on myoglobin

http://www.wikidata.org/entity/Q27660923

description

2010 nî lūn-bûn

@nan

2010 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի մայիսին 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

Roles of glutamates and metal ...... e reductase based on myoglobin

@ast

Roles of glutamates and metal ...... e reductase based on myoglobin

@en

Roles of glutamates and metal ...... e reductase based on myoglobin

@nl

type

label

Roles of glutamates and metal ...... e reductase based on myoglobin

@ast

Roles of glutamates and metal ...... e reductase based on myoglobin

@en

Roles of glutamates and metal ...... e reductase based on myoglobin

@nl

prefLabel

Roles of glutamates and metal ...... e reductase based on myoglobin

@ast

Roles of glutamates and metal ...... e reductase based on myoglobin

@en

Roles of glutamates and metal ...... e reductase based on myoglobin

@nl

P1433

Q27660923-7042405D-631C-4E6A-B244-2092B0212C70

P1476

Q27660923-B714A2FD-A847-44A0-8C01-0874B9BF618D

P2093

Q27660923-0EE5D038-13AD-44BA-962A-5DF29D97AC82

Q27660923-B948A374-D8F7-4C06-922B-51145BB1F483

Q27660923-BB1F6F28-80F7-4705-B8AD-FF3CDAE24E14

Q27660923-C3DC1E4F-DC8D-4885-82D7-2ADEBE3A41A5

Q27660923-C9F24FF1-FA39-41FA-9328-E22E00623C95

Q27660923-D8F24992-65BD-4C8C-9BCA-22B39EDE78D5

P2860

Q27660923-03A767F2-5E66-4092-8934-D50C9927470D

Q27660923-085149C0-3998-457F-B44C-CC75808FE90F

Q27660923-1181684E-EDFD-4678-97C5-B6869E7ACAF8

Q27660923-14902F0E-37B0-487D-8161-EC19CEF768A1

Q27660923-1B4EF8C0-2FF6-4B13-840D-7F24D8A87565

Q27660923-1E15BF1B-9A98-416D-890C-4B7B3937BA37

Q27660923-21115E9B-F0A3-4A20-BCC5-EDD051B4166C

Q27660923-259D4402-E962-4C8E-B0DB-FE4A07DC4DAE

Q27660923-28F62B76-93CF-432F-8A1F-3B32C6D459DA

Q27660923-3BE3EBB9-D491-4F65-A05D-EE68AC9887BF

P304

Q27660923-25044BEC-ABB2-4F51-863A-BB3D9A00442E

P31

Q27660923-BA1345A7-085A-4F02-A79C-98B4960E2229

P356

Q27660923-A130C3A4-73A0-4941-A18C-72D7AE3C47A6

P407

Q27660923-BA18484E-7608-4535-92BD-E057F591A020

P433

Q27660923-B2B34164-2801-4E52-84B5-1E732A0C9ABB

P478

Q27660923-88261832-EDBA-4175-BF0C-15DDDCD4F8E0

P50

Q27660923-3ABF63C2-4A2E-4404-8715-5E2598D24411

P577

Q27660923-B6AEC023-5A16-48BF-B704-7154B1282B88

P5875

Q27660923-4CEAB239-5477-49BB-BD98-48AC4BA08FF5

P698

Q27660923-209285B9-9792-41B4-8B52-B9CB5F030DAB

P932

Q27660923-7F04DE30-9EE7-40DA-AF5A-F4EE4B59107C

P356

PNAS.1000526107

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Roles of glutamates and metal ...... e reductase based on myoglobin

@en

P2093

Howard Robinson

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

Kyle D Miner

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

Natasha Yeung

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

Shiliang Tian

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

Yi-Gui Gao

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

Ying-Wu Lin

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

P2860

De novo computational design of retro-aldol enzymes

Design and engineering of an O(2) transport protein

Rationally tuning the reduction potential of a single cupredoxin beyond the natural range

Rational design of a structural and functional nitric oxide reductase

Characterization of a helical protein designed from first principles

Designing artificial enzymes by intuition and computation

Proton and electron pathways in the bacterial nitric oxide reductase.

Computational protein design: structure, function and combinatorial diversity.

Heme protein assemblies.

NO reduction by nitric-oxide reductase from denitrifying bacterium Pseudomonas aeruginosa: characterization of reaction intermediates that appear in the single turnover cycle.

P304

8581-6

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

P31

scholarly article

P356

10.1073/PNAS.1000526107

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

P407

P433

19

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

P478

107

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

P50

P577

2010-05-11T00:00:00Z

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

P5875

43345717

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

P698

20421510

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

P932

2889330

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