Loading…

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

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 p...

Full description

Saved in:
Bibliographic Details
Published in:Metallomics 2011-02, Vol.3 (2), p.140-151
Main Authors: Choi, Moonsung, Davidson, Victor L
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c443t-222d74b288f9d1c5843cf319c26c6be2bbcff85e32d2bba2b47882c0e2346bd43
cites cdi_FETCH-LOGICAL-c443t-222d74b288f9d1c5843cf319c26c6be2bbcff85e32d2bba2b47882c0e2346bd43
container_end_page 151
container_issue 2
container_start_page 140
container_title Metallomics
container_volume 3
creator Choi, Moonsung
Davidson, Victor L
description 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.
doi_str_mv 10.1039/c0mt00061b
format article
fullrecord <record><control><sourceid>pubmed_cross</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6916721</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>21258692</sourcerecordid><originalsourceid>FETCH-LOGICAL-c443t-222d74b288f9d1c5843cf319c26c6be2bbcff85e32d2bba2b47882c0e2346bd43</originalsourceid><addsrcrecordid>eNpVkF1LwzAYhYMobk5v_AGSa6Gar6btjSBjfsDAG4XdhSZ9s1XWpiTpdP_ejunUq_fAec554SB0SckNJby4NaSJhBBJ9REa0yyVSVrQxfFBEzpCZyG8D4ggJD1FI0ZZmsuCjdFi2nceKvdZtyFJShxiX22xs3jlPnDnXYTBwE25xbBx6w3g6HAfADcQy3XA1nmsawct-CXE2uwiBkKAcI5O7EDAxfedoLeH2ev0KZm_PD5P7-eJEYLHhDFWZUKzPLdFRU2aC24sp4Vh0kgNTGtjbZ4CZ9WgS6ZFlufMEGBcSF0JPkF3-96u1w1UBtroy7XqfN2UfqtcWav_Tluv1NJtlCyozBgdCq73Bca7EDzYQ5YStdtX_e47wFd_vx3Qn0H5F-AEeWc</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Cupredoxins--a study of how proteins may evolve to use metals for bioenergetic processes</title><source>Oxford University Press:Jisc Collections:OUP Read and Publish 2024-2025 (2024 collection) (Reading list)</source><creator>Choi, Moonsung ; Davidson, Victor L</creator><creatorcontrib>Choi, Moonsung ; Davidson, Victor L</creatorcontrib><description>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.</description><identifier>ISSN: 1756-5901</identifier><identifier>EISSN: 1756-591X</identifier><identifier>DOI: 10.1039/c0mt00061b</identifier><identifier>PMID: 21258692</identifier><language>eng</language><publisher>England</publisher><subject>Azurin - chemistry ; Azurin - metabolism ; Binding Sites ; Copper - chemistry ; Copper - metabolism ; Models, Molecular ; Plastocyanin - chemistry ; Plastocyanin - metabolism</subject><ispartof>Metallomics, 2011-02, Vol.3 (2), p.140-151</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c443t-222d74b288f9d1c5843cf319c26c6be2bbcff85e32d2bba2b47882c0e2346bd43</citedby><cites>FETCH-LOGICAL-c443t-222d74b288f9d1c5843cf319c26c6be2bbcff85e32d2bba2b47882c0e2346bd43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21258692$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Choi, Moonsung</creatorcontrib><creatorcontrib>Davidson, Victor L</creatorcontrib><title>Cupredoxins--a study of how proteins may evolve to use metals for bioenergetic processes</title><title>Metallomics</title><addtitle>Metallomics</addtitle><description>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.</description><subject>Azurin - chemistry</subject><subject>Azurin - metabolism</subject><subject>Binding Sites</subject><subject>Copper - chemistry</subject><subject>Copper - metabolism</subject><subject>Models, Molecular</subject><subject>Plastocyanin - chemistry</subject><subject>Plastocyanin - metabolism</subject><issn>1756-5901</issn><issn>1756-591X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><recordid>eNpVkF1LwzAYhYMobk5v_AGSa6Gar6btjSBjfsDAG4XdhSZ9s1XWpiTpdP_ejunUq_fAec554SB0SckNJby4NaSJhBBJ9REa0yyVSVrQxfFBEzpCZyG8D4ggJD1FI0ZZmsuCjdFi2nceKvdZtyFJShxiX22xs3jlPnDnXYTBwE25xbBx6w3g6HAfADcQy3XA1nmsawct-CXE2uwiBkKAcI5O7EDAxfedoLeH2ev0KZm_PD5P7-eJEYLHhDFWZUKzPLdFRU2aC24sp4Vh0kgNTGtjbZ4CZ9WgS6ZFlufMEGBcSF0JPkF3-96u1w1UBtroy7XqfN2UfqtcWav_Tluv1NJtlCyozBgdCq73Bca7EDzYQ5YStdtX_e47wFd_vx3Qn0H5F-AEeWc</recordid><startdate>201102</startdate><enddate>201102</enddate><creator>Choi, Moonsung</creator><creator>Davidson, Victor L</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>5PM</scope></search><sort><creationdate>201102</creationdate><title>Cupredoxins--a study of how proteins may evolve to use metals for bioenergetic processes</title><author>Choi, Moonsung ; Davidson, Victor L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c443t-222d74b288f9d1c5843cf319c26c6be2bbcff85e32d2bba2b47882c0e2346bd43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Azurin - chemistry</topic><topic>Azurin - metabolism</topic><topic>Binding Sites</topic><topic>Copper - chemistry</topic><topic>Copper - metabolism</topic><topic>Models, Molecular</topic><topic>Plastocyanin - chemistry</topic><topic>Plastocyanin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Choi, Moonsung</creatorcontrib><creatorcontrib>Davidson, Victor L</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Metallomics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Choi, Moonsung</au><au>Davidson, Victor L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cupredoxins--a study of how proteins may evolve to use metals for bioenergetic processes</atitle><jtitle>Metallomics</jtitle><addtitle>Metallomics</addtitle><date>2011-02</date><risdate>2011</risdate><volume>3</volume><issue>2</issue><spage>140</spage><epage>151</epage><pages>140-151</pages><issn>1756-5901</issn><eissn>1756-591X</eissn><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.</abstract><cop>England</cop><pmid>21258692</pmid><doi>10.1039/c0mt00061b</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 1756-5901
ispartof Metallomics, 2011-02, Vol.3 (2), p.140-151
issn 1756-5901
1756-591X
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6916721
source Oxford University Press:Jisc Collections:OUP Read and Publish 2024-2025 (2024 collection) (Reading list)
subjects Azurin - chemistry
Azurin - metabolism
Binding Sites
Copper - chemistry
Copper - metabolism
Models, Molecular
Plastocyanin - chemistry
Plastocyanin - metabolism
title Cupredoxins--a study of how proteins may evolve to use metals for bioenergetic processes
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T22%3A30%3A46IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-pubmed_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Cupredoxins--a%20study%20of%20how%20proteins%20may%20evolve%20to%20use%20metals%20for%20bioenergetic%20processes&rft.jtitle=Metallomics&rft.au=Choi,%20Moonsung&rft.date=2011-02&rft.volume=3&rft.issue=2&rft.spage=140&rft.epage=151&rft.pages=140-151&rft.issn=1756-5901&rft.eissn=1756-591X&rft_id=info:doi/10.1039/c0mt00061b&rft_dat=%3Cpubmed_cross%3E21258692%3C/pubmed_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c443t-222d74b288f9d1c5843cf319c26c6be2bbcff85e32d2bba2b47882c0e2346bd43%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_id=info:pmid/21258692&rfr_iscdi=true