Literature DB >> 21258692

Cupredoxins--a study of how proteins may evolve to use metals for bioenergetic processes.

Moonsung Choi1, Victor L Davidson.   

Abstract

Cupredoxins are small proteins that contain type I copper centers, which are ubiquitous in nature. They function as electron transfer shuttles between proteins. This review of the structure and properties of native cupredoxins, and those modified by site-directed mutagenesis, illustrates how these proteins may have evolved to specifically bind copper, develop recognition sites for specific redox partners, tune redox potential for a particular function, and allow for efficient electron transfer through the protein matrix. This is relevant to the general understanding of the roles of metals in energy metabolism, respiration and photosynthesis.

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Year:  2011        PMID: 21258692      PMCID: PMC6916721          DOI: 10.1039/c0mt00061b

Source DB:  PubMed          Journal:  Metallomics        ISSN: 1756-5901            Impact factor:   4.526


  84 in total

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Journal:  Nature       Date:  1999-11-04       Impact factor: 49.962

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3.  Surface residues dynamically organize water bridges to enhance electron transfer between proteins.

Authors:  Aurélien de la Lande; Nathan S Babcock; Jan Rezác; Barry C Sanders; Dennis R Salahub
Journal:  Proc Natl Acad Sci U S A       Date:  2010-06-14       Impact factor: 11.205

4.  Complex formation with methylamine dehydrogenase affects the pathway of electron transfer from amicyanin to cytochrome c-551i.

Authors:  V L Davidson; L H Jones
Journal:  J Biol Chem       Date:  1995-10-13       Impact factor: 5.157

5.  Novel insight into the copper-ligand geometry in the crystal structure of Ulva pertusa plastocyanin at 1.6-A resolution. Structural basis for regulation of the copper site by residue 88.

Authors:  N Shibata; T Inoue; C Nagano; N Nishio; T Kohzuma; K Onodera; F Yoshizaki; Y Sugimura; Y Kai
Journal:  J Biol Chem       Date:  1999-02-12       Impact factor: 5.157

6.  Spectroscopic evidence for a common electron transfer pathway for two tryptophan tryptophylquinone enzymes.

Authors:  S L Edwards; V L Davidson; Y L Hyun; P T Wingfield
Journal:  J Biol Chem       Date:  1995-03-03       Impact factor: 5.157

7.  Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. A pH-induced conformational transition involves a peptide bond flip.

Authors:  H Nar; A Messerschmidt; R Huber; M van de Kamp; G W Canters
Journal:  J Mol Biol       Date:  1991-10-05       Impact factor: 5.469

8.  Preparation and spectroscopic studies of cobalt(II)-stellacyanin.

Authors:  D R McMillin; R A Holwerda; H B Gray
Journal:  Proc Natl Acad Sci U S A       Date:  1974-04       Impact factor: 11.205

9.  The crystal structure of nickel(II)-azurin.

Authors:  J M Moratal; A Romero; J Salgado; A Perales-Alarcón; H R Jiménez
Journal:  Eur J Biochem       Date:  1995-03-15

10.  Bacterial cupredoxin azurin as an inducer of apoptosis and regression in human breast cancer.

Authors:  Vasu Punj; Suchita Bhattacharyya; Djenann Saint-Dic; Chenthamarakshan Vasu; Elizabeth A Cunningham; Jewell Graves; Tohru Yamada; Andreas I Constantinou; Konstantin Christov; Bethany White; Gang Li; Dibyen Majumdar; Ananda M Chakrabarty; Tapas K Das Gupta
Journal:  Oncogene       Date:  2004-03-25       Impact factor: 9.867

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  28 in total

1.  Replacement of the axial copper ligand methionine with lysine in amicyanin converts it to a zinc-binding protein that no longer binds copper.

Authors:  Narayanasami Sukumar; Moonsung Choi; Victor L Davidson
Journal:  J Inorg Biochem       Date:  2011-08-12       Impact factor: 4.155

Review 2.  Elemental economy: microbial strategies for optimizing growth in the face of nutrient limitation.

Authors:  Sabeeha S Merchant; John D Helmann
Journal:  Adv Microb Physiol       Date:  2012       Impact factor: 3.517

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

Authors:  Parisa Hosseinzadeh; Nicholas M Marshall; Kelly N Chacón; Yang Yu; Mark J Nilges; Siu Yee New; Stoyan A Tashkov; Ninian J Blackburn; Yi Lu
Journal:  Proc Natl Acad Sci U S A       Date:  2015-12-02       Impact factor: 11.205

4.  Copper Oxidation/Reduction in Water and Protein: Studies with DFTB3/MM and VALBOND Molecular Dynamics Simulations.

Authors:  Haiyun Jin; Puja Goyal; Akshaya Kumar Das; Michael Gaus; Markus Meuwly; Qiang Cui
Journal:  J Phys Chem B       Date:  2015-12-17       Impact factor: 2.991

5.  The X-ray absorption spectroscopic model of the copper(II) imidazole complex ion in liquid aqueous solution: a strongly solvated square pyramid.

Authors:  Patrick Frank; Maurizio Benfatto; Britt Hedman; Keith O Hodgson
Journal:  Inorg Chem       Date:  2012-02-08       Impact factor: 5.165

6.  A simple method to engineer a protein-derived redox cofactor for catalysis.

Authors:  Sooim Shin; Moonsung Choi; Heather R Williamson; Victor L Davidson
Journal:  Biochim Biophys Acta       Date:  2014-05-22

7.  Effect of circular permutation on the structure and function of type 1 blue copper center in azurin.

Authors:  Yang Yu; Igor D Petrik; Kelly N Chacón; Parisa Hosseinzadeh; Honghui Chen; Ninian J Blackburn; Yi Lu
Journal:  Protein Sci       Date:  2016-11-04       Impact factor: 6.725

Review 8.  miRNomes involved in imparting thermotolerance to crop plants.

Authors:  Vijay Gahlaut; Vinay Kumar Baranwal; Paramjit Khurana
Journal:  3 Biotech       Date:  2018-11-24       Impact factor: 2.406

Review 9.  Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.

Authors:  Jing Liu; Saumen Chakraborty; Parisa Hosseinzadeh; Yang Yu; Shiliang Tian; Igor Petrik; Ambika Bhagi; Yi Lu
Journal:  Chem Rev       Date:  2014-04-23       Impact factor: 60.622

10.  Periplasmic Nicotine Dehydrogenase NdhAB Utilizes Pseudoazurin as Its Physiological Electron Acceptor in Agrobacterium tumefaciens S33.

Authors:  Wenjun Yu; Rongshui Wang; Haiyan Huang; Huijun Xie; Shuning Wang
Journal:  Appl Environ Microbiol       Date:  2017-08-17       Impact factor: 4.792

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