Systematic Tuning of Heme Redox Potentials and Its Effects on O 2 Reduction Rates in a Designed Oxidase in Myoglobin - Wikidata - awgldk - TriplyDB

Systematic Tuning of Heme Redox Potentials and Its Effects on O 2 Reduction Rates in a Designed Oxidase in Myoglobin

Systematic Tuning of Heme Redox Potentials and Its Effects on O 2 Reduction Rates in a Designed Oxidase in Myoglobin

http://www.wikidata.org/entity/Q27684883

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Heme biomolecule as redox mediator and oxygen shuttle for efficient charging of lithium-oxygen batteries Designed metalloprotein stabilizes a semiquinone radical Highly diastereoselective and enantioselective olefin cyclopropanation using engineered myoglobin-based catalysts.Intermolecular carbene S-H insertion catalysed by engineered myoglobin-based catalysts†.A biosynthetic model of cytochrome c oxidase as an electrocatalyst for oxygen reduction.A Designed Metalloenzyme Achieving the Catalytic Rate of a Native Enzyme.Design of a single protein that spans the entire 2-V range of physiological redox potentials Spectroscopic and Crystallographic Evidence for the Role of a Water-Containing H-Bond Network in Oxidase Activity of an Engineered Myoglobin.Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics.Structural Characterization of Heme Environmental Mutants of CgHmuT that Shuttles Heme Molecules to Heme Transporters Design of Heteronuclear Metalloenzymes.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.Reactivity Descriptors for the Activity of Molecular MN4 Catalysts for the Oxygen Reduction Reaction.Improving artificial metalloenzymes' activity by optimizing electron transfer.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.Cyclopropanations via Heme Carbenes: Basic Mechanism and Effects of Carbene Substituent, Protein Axial Ligand, and Porphyrin Substitution.Insights Into How Heme Reduction Potentials Modulate Enzymatic Activities of a Myoglobin-based Functional Oxidase.

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P2860

Systematic Tuning of Heme Redox Potentials and Its Effects on O 2 Reduction Rates in a Designed Oxidase in Myoglobin

http://www.wikidata.org/entity/Q27684883

description

2014 nî lūn-bûn

@nan

2014 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2014年の論文

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2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

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name

Systematic Tuning of Heme Redo ...... Designed Oxidase in Myoglobin

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Systematic Tuning of Heme Redo ...... Designed Oxidase in Myoglobin

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Systematic Tuning of Heme Redo ...... Designed Oxidase in Myoglobin

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type

label

Systematic Tuning of Heme Redo ...... Designed Oxidase in Myoglobin

@ast

Systematic Tuning of Heme Redo ...... Designed Oxidase in Myoglobin

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Systematic Tuning of Heme Redo ...... Designed Oxidase in Myoglobin

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Systematic Tuning of Heme Redo ...... Designed Oxidase in Myoglobin

@ast

Systematic Tuning of Heme Redo ...... Designed Oxidase in Myoglobin

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Systematic Tuning of Heme Redo ...... Designed Oxidase in Myoglobin

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Journal of the American Chemical Society

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Systematic Tuning of Heme Redo ...... Designed Oxidase in Myoglobin

@en

P2093

Ambika Bhagi-Damodaran

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Howard Robinson

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

Igor D Petrik

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

Nicholas M Marshall

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

P2860

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

A Designed Functional Metalloenzyme that Reduces O2 to H2O with Over One Thousand Turnovers

Development of a heme protein structure-electrochemical function database.

Spectroscopic study of Ser92 mutants of human myoglobin: hydrogen bonding effect of Ser92 to proximal His93 on structure and property of myoglobin.

Facile, scalable synthesis of edge-halogenated graphene nanoplatelets as efficient metal-free eletrocatalysts for oxygen reduction reaction.

Heme-Cu complexes as oxygen-activating functional models for the active site of cytochrome c oxidase.

Faster interprotein electron transfer in a [myoglobin, b⁵] complex with a redesigned interface.

Construction of heme enzymes: four approaches.

Redox-controlled proton gating in bovine cytochrome c oxidase

The role of copper and protons in heme-copper oxidases: kinetic study of an engineered heme-copper center in myoglobin.

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11882-5

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scholarly article

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1237122

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10.1021/JA5054863

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34

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136

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2014-08-27T00:00:00Z

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264392045

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25076049

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4151708

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