| pubmed-article:1353610 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1353610 | lifeskim:mentions | umls-concept:C0038838 | lld:lifeskim |
| pubmed-article:1353610 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:1353610 | lifeskim:mentions | umls-concept:C1959633 | lld:lifeskim |
| pubmed-article:1353610 | lifeskim:mentions | umls-concept:C1999177 | lld:lifeskim |
| pubmed-article:1353610 | lifeskim:mentions | umls-concept:C1707689 | lld:lifeskim |
| pubmed-article:1353610 | pubmed:issue | 6384 | lld:pubmed |
| pubmed-article:1353610 | pubmed:dateCreated | 1992-8-28 | lld:pubmed |
| pubmed-article:1353610 | pubmed:abstractText | The enzyme Cu, Zn superoxide dismutase (SOD) protects against oxidative damage by dismuting the superoxide radical O2-. to molecular oxygen and hydrogen peroxide at the active-site Cu ion in a reaction that is rate-limited by diffusion and enhanced by electrostatic guidance. SOD has evolved to be one of the fastest enzymes known (V(max) approximately 2 x 10(9) M-1 s-1). The new crystal structures of human SOD show that amino-acid site chains that are implicated in electrostatic guidance (Glu 132, Glu 133 and Lys 136) form a hydrogen-bonding network. Here we show that site-specific mutants that increase local positive charge while maintaining this orienting network (Glu----Gln) have faster reaction rates and increased ionic-strength dependence, matching brownian dynamics simulations incorporating electrostatic terms. Increased positive charge alone is insufficient: one charge reversal (Glu----Lys) mutant is slower than the equivalent charge neutralization (Glu----Gln) mutant, showing that the newly introduced positive charge disrupts the orienting network. Thus, electrostatically facilitated diffusion rates can be increased by design, provided the detailed structural integrity of the active-site electrostatic network is maintained. | lld:pubmed |
| pubmed-article:1353610 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1353610 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1353610 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1353610 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1353610 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1353610 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1353610 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1353610 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1353610 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:1353610 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:1353610 | pubmed:author | pubmed-author:GetzoffE DED | lld:pubmed |
| pubmed-article:1353610 | pubmed:author | pubmed-author:HallewellR... | lld:pubmed |
| pubmed-article:1353610 | pubmed:author | pubmed-author:BanciLL | lld:pubmed |
| pubmed-article:1353610 | pubmed:author | pubmed-author:FisherC LCL | lld:pubmed |
| pubmed-article:1353610 | pubmed:author | pubmed-author:PargeH EHE | lld:pubmed |
| pubmed-article:1353610 | pubmed:author | pubmed-author:CabelliD EDE | lld:pubmed |
| pubmed-article:1353610 | pubmed:author | pubmed-author:ViezzoliM SMS | lld:pubmed |
| pubmed-article:1353610 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1353610 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:1353610 | pubmed:volume | 358 | lld:pubmed |
| pubmed-article:1353610 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1353610 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1353610 | pubmed:pagination | 347-51 | lld:pubmed |
| pubmed-article:1353610 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:1353610 | pubmed:meshHeading | pubmed-meshheading:1353610-... | lld:pubmed |
| pubmed-article:1353610 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1353610 | pubmed:articleTitle | Faster superoxide dismutase mutants designed by enhancing electrostatic guidance. | lld:pubmed |
| pubmed-article:1353610 | pubmed:affiliation | Department of Molecular Biology, Scripps Research Institute, La Jolla, California 92037. | lld:pubmed |
| pubmed-article:1353610 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1353610 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1353610 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:1353610 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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