Design of a single protein that spans the entire 2-V range of physiological redox potentials

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

Volumn 113, Issue 2, 2016, Pages 262-267

  Hosseinzadeh, Parisa ^a   Marshall, Nicholas M ^b   Chacón, Kelly N ^c,d   Yu, Yang ^a   Nilges, Mark J ^a,b   New, Siu Yee ^a   Tashkov, Stoyan A ^e   Blackburn, Ninian J ^c   Lu, Yi ^a,b  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^b UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^c OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^d REED COLLEGE   (United States)

^e United States of America   (United States)

Author keywords

Azurin; Cupredoxins; Electron transfer; Reduction potential; Secondary coordination sphere

Indexed keywords

AZURIN;

ARTICLE; BIOPHYSICS; ELECTRON TRANSPORT; HYDROGEN BOND; HYDROPHOBICITY; METAL BINDING; OXIDATION REDUCTION POTENTIAL; OXIDATION REDUCTION REACTION; PH ELECTRODE; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTEIN UNFOLDING; SURFACE PROPERTY; CHEMISTRY; ELECTROCHEMICAL ANALYSIS; ELECTRON SPIN RESONANCE; GENETICS; METABOLISM; MOLECULAR MODEL; MUTATION; PROTEIN ENGINEERING; SPECTROMETRY; ULTRAVIOLET SPECTROPHOTOMETRY;

AZURIN; ELECTROCHEMICAL TECHNIQUES; ELECTRON SPIN RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MUTATION; OXIDATION-REDUCTION; PROTEIN ENGINEERING; SPECTROMETRY, X-RAY EMISSION; SPECTROPHOTOMETRY, ULTRAVIOLET;

EID: 84954539922     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1515897112     Document Type: Article

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