Roles of glutamates and metal ions in a rationally designed nitric oxide reductase based on myoglobin
about
Beyond directed evolution--semi-rational protein engineering and designProtein design: toward functional metalloenzymesIntroducing a 2-His-1-Glu Nonheme Iron Center into Myoglobin Confers Nitric Oxide Reductase ActivityStructural basis of biological N2O generation by bacterial nitric oxide reductaseAzurin as a Protein Scaffold for a Low-coordinate Nonheme Iron Site with a Small-molecule Binding PocketCrystal structure of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilusSpectroscopic and Computational Study of a Nonheme Iron Nitrosyl Center in a Biosynthetic Model of Nitric Oxide ReductaseRational design of heterodimeric protein using domain swapping for myoglobinEnhancing Mn(II)-Binding and Manganese Peroxidase Activity in a Designed Cytochrome c Peroxidase through Fine-Tuning Secondary-Sphere InteractionsDistinct roles of a tyrosine-associated hydrogen-bond network in fine-tuning the structure and function of heme proteins: two cases designed for myoglobinCharacterization 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 reductaseHighly 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 functionsA 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 myoglobinDesign and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics.Myoglobin-Catalyzed Olefination of AldehydesBiotinylated Rh(III) complexes in engineered streptavidin for accelerated asymmetric C-H activationDesign 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 ReductasesProtein 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
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P2860
Roles of glutamates and metal ions in a rationally designed nitric oxide reductase based on myoglobin
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
P2093
P2860
P356
P1476
Roles of glutamates and metal ...... e reductase based on myoglobin
@en
P2093
Howard Robinson
Kyle D Miner
Natasha Yeung
Shiliang Tian
Yi-Gui Gao
Ying-Wu Lin
P2860
P304
P356
10.1073/PNAS.1000526107
P407
P50
P577
2010-05-11T00:00:00Z