The selenocysteine-substituted blue copper center: spectroscopic investigations of Cys112SeCys Pseudomonas aeruginosa azurin.
about
Protein design: toward functional metalloenzymesInner- and outer-sphere metal coordination in blue copper proteinsInteractions of Cu(I) with selenium-containing amino acids determined by NMR, XAS, and DFT studies.Transforming a blue copper into a red copper protein: engineering cysteine and homocysteine into the axial position of azurin using site-directed mutagenesis and expressed protein ligation.Metallopeptide catalysts and artificial metalloenzymes containing unnatural amino acidsSynthesis of single- and multiple-stranded cystine-rich peptides.Incorporation of selenocysteine into proteins using peptide ligationStudies on deprotection of cysteine and selenocysteine side-chain protecting groups.Nitrite Reductase Activity in Engineered Azurin VariantsSpectroscopic and density functional theory studies of the blue-copper site in M121SeM and C112SeC azurin: Cu-Se versus Cu-S bonding.Selenolate complexes of CYP101 and the heme-bound hHO-1/H25A proximal cavity mutantExpressed protein ligation for metalloprotein design and engineering.Modulating the Copper-Sulfur Interaction in Type 1 Blue Copper Azurin by Replacing Cys112 with Nonproteinogenic Homocysteine.Metalloproteins containing cytochrome, iron-sulfur, or copper redox centersDevelopments and recent advancements in the field of endogenous amino acid selective bond forming reactions for bioconjugation.Accessing human selenoproteins through chemical protein synthesis.Metalloprotein and metallo-DNA/RNAzyme design: current approaches, success measures, and future challenges.Synthetic seleno-glutaredoxin 3 analogues are highly reducing oxidoreductases with enhanced catalytic efficiency.High-potential C112D/M121X (X = M, E, H, L) Pseudomonas aeruginosa azurins.Traceless ligation of cysteine peptides using selective deselenization.Selenite-mediated production of superoxide radical anions in A549 cancer cells is accompanied by a selective increase in SOD1 concentration, enhanced apoptosis and Se-Cu bonding.Probing the role of the backbone carbonyl interaction with the CuA center in azurin by replacing the peptide bond with an ester linkage.Incorporation of the red copper nitrosocyanin binding loop into blue copper azurin.Biosynthetic approach to modeling and understanding metalloproteins using unnatural amino acidsInvestigating the Structural, Spectroscopic, and Electrochemical Properties of [Fe{(EPiPr2)2N}2] (E = S, Se) and the Formation of Iron Selenides by Chemical Vapor Deposition
P2860
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P2860
The selenocysteine-substituted blue copper center: spectroscopic investigations of Cys112SeCys Pseudomonas aeruginosa azurin.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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2004年学术文章
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2004年学术文章
@zh-my
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name
The selenocysteine-substituted ...... Pseudomonas aeruginosa azurin.
@en
The selenocysteine-substituted ...... Pseudomonas aeruginosa azurin.
@nl
type
label
The selenocysteine-substituted ...... Pseudomonas aeruginosa azurin.
@en
The selenocysteine-substituted ...... Pseudomonas aeruginosa azurin.
@nl
prefLabel
The selenocysteine-substituted ...... Pseudomonas aeruginosa azurin.
@en
The selenocysteine-substituted ...... Pseudomonas aeruginosa azurin.
@nl
P2093
P356
P1476
The selenocysteine-substituted ...... Pseudomonas aeruginosa azurin.
@en
P2093
Mark J Nilges
Martina Ralle
Matt D Gieselman
Ninian J Blackburn
Steven M Berry
P304
P356
10.1021/JA031821H
P407
P577
2004-06-01T00:00:00Z