Modulating Heme Redox Potential through Protein-Induced Porphyrin Distortion

scientific article

Modulating Heme Redox Potential through Protein-Induced Porphyrin Distortion is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1021/JA106252B
P932PMC publication ID2939930
P698PubMed publication ID20735135
P5875ResearchGate publication ID45826497

P50authorJohn KuriyanQ6243502
P2093author name stringMichael A Marletta
Charles Olea
P2860cites workProbing the Function of Heme Distortion in the H-NOX FamilyQ27652988
The reduction potential of cytochrome b5 is modulated by its exposed heme edgeQ27748873
Development of a heme protein structure-electrochemical function database.Q30365156
Structure-function relationships in heme-proteinsQ34131172
Conservation of the conformation of the porphyrin macrocycle in hemoproteinsQ34179945
Metalloprotein and redox protein designQ34331494
Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclasesQ37511692
Electrostatic control of midpoint potentials in the cytochrome subunit of the Rhodopseudomonas viridis reaction centerQ37607518
Resonance Raman spectra of an O2-binding H-NOX domain reveal heme relaxation upon mutationQ42549246
Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systemsQ43834034
Control of cytochrome C redox potential: axial ligation and protein environment effectsQ43983721
Influence of electronic and structural effects on the oxidative behavior of nickel porphyrinsQ44241255
Protein folding triggered by electron transferQ46116036
Modulation of metal displacements in a saddle distorted macrocycle: synthesis, structure, and properties of high-spin Fe(III) porphyrins and implications for the hemoproteinsQ46431714
Protein-induced changes in nonplanarity of the porphyrin in nickel cytochrome c probed by resonance Raman spectroscopy.Q51647623
Heme redox potential control in de novo designed four-alpha-helix bundle proteinsQ57135297
Effects of buried ionizable amino acids on the reduction potential of recombinant myoglobinQ66778010
Extension of the fragment method to calculate amino acid zwitterion and side chain partition coefficientsQ68697921
Control of the redox potential in c-type cytochromes: importance of the entropic contributionQ72046573
How cytochromes with different folds control heme redox potentialsQ73821156
Insight into heme protein redox potential control and functional aspects of six-coordinate ligand-sensing heme proteins from studies of synthetic heme peptidesQ79398717
P433issue37
P407language of work or nameEnglishQ1860
P921main subjectcatalysisQ82264
P304page(s)12794-5
P577publication date2010-09-22
P1433published inJournal of the American Chemical SocietyQ898902
P1476titleModulating Heme Redox Potential through Protein-Induced Porphyrin Distortion
P478volume132

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cites work (P2860)
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Q27670635Controlling Conformational Flexibility of an O 2 -Binding H-NOX Domain
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Q38780554Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities

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