| pubmed-article:12501184 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12501184 | lifeskim:mentions | umls-concept:C0205474 | lld:lifeskim |
| pubmed-article:12501184 | lifeskim:mentions | umls-concept:C0028174 | lld:lifeskim |
| pubmed-article:12501184 | lifeskim:mentions | umls-concept:C0184512 | lld:lifeskim |
| pubmed-article:12501184 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:12501184 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
| pubmed-article:12501184 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:12501184 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:12501184 | lifeskim:mentions | umls-concept:C0537374 | lld:lifeskim |
| pubmed-article:12501184 | pubmed:issue | 52 | lld:pubmed |
| pubmed-article:12501184 | pubmed:dateCreated | 2002-12-26 | lld:pubmed |
| pubmed-article:12501184 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12501184 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12501184 | pubmed:abstractText | The transient formation of a complex between the component Fe- and MoFe-proteins of nitrogenase represents a central event in the substrate reduction mechanism of this enzyme. Previously, we have isolated an N-[3-(dimethylamino)propyl]-N'-ethylcarbodiimide (EDC) cross-linked complex of these proteins stabilized by a covalent isopeptide linkage between Glu 112 and Lys beta400 of the Fe-protein and MoFe-protein, respectively [Willing, A., et al. (1989) J. Biol. Chem. 264, 8499-8503; Willing, A., and Howard, J. B. (1990) J. Biol. Chem. 265, 6596-6599]. We report here the biochemical and structural characterization of the cross-linked complex to assess the mechanistic relevance of this species. Glycinamide inhibits the cross-linking reaction, and is found to be specifically incorporated into Glu 112 of the Fe-protein, without detectable modification of either of the neighboring residues (Glu 110 and Glu 111). This modified protein is still competent for substrate reduction, demonstrating that formation of the cross-linked complex is responsible for the enzymatic inactivation, and not the EDC reaction or the modification of the Fe-protein. Crystallographic analysis of the EDC-cross-linked complex at 3.2 A resolution confirms the site of the isopeptide linkage. The nature of the protein surfaces around the cross-linking site suggests there is a strong electrostatic component to the formation of the complex, although the interface area between the component proteins is small. The binding footprints between proteins in the cross-linked complex are adjacent, but with little overlap, to those observed in the complex of the nitrogenase proteins stabilized by ADP-AlF(4)(-). The results of these studies suggest that EDC cross-linking traps a nucleotide-independent precomplex of the nitrogenase proteins driven by complementary electrostatic interactions that subsequently rearranges in a nucleotide-dependent fashion to the electron transfer competent state observed in the ADP-AlF(4)(-) structure. | lld:pubmed |
| pubmed-article:12501184 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12501184 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12501184 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12501184 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12501184 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12501184 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12501184 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12501184 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12501184 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12501184 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12501184 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12501184 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12501184 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12501184 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12501184 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12501184 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12501184 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12501184 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:12501184 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:12501184 | pubmed:author | pubmed-author:EinsleOliverO | lld:pubmed |
| pubmed-article:12501184 | pubmed:author | pubmed-author:ReesDouglas... | lld:pubmed |
| pubmed-article:12501184 | pubmed:author | pubmed-author:SchmidBenedik... | lld:pubmed |
| pubmed-article:12501184 | pubmed:author | pubmed-author:YoshidaMikaM | lld:pubmed |
| pubmed-article:12501184 | pubmed:author | pubmed-author:HowardJames... | lld:pubmed |
| pubmed-article:12501184 | pubmed:author | pubmed-author:ChiuHsiu-JuHJ | lld:pubmed |
| pubmed-article:12501184 | pubmed:author | pubmed-author:WillingAndrea... | lld:pubmed |
| pubmed-article:12501184 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12501184 | pubmed:day | 31 | lld:pubmed |
| pubmed-article:12501184 | pubmed:volume | 41 | lld:pubmed |
| pubmed-article:12501184 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12501184 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12501184 | pubmed:pagination | 15557-65 | lld:pubmed |
| pubmed-article:12501184 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:12501184 | pubmed:meshHeading | pubmed-meshheading:12501184... | lld:pubmed |
| pubmed-article:12501184 | pubmed:meshHeading | pubmed-meshheading:12501184... | lld:pubmed |
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| pubmed-article:12501184 | pubmed:meshHeading | pubmed-meshheading:12501184... | lld:pubmed |
| pubmed-article:12501184 | pubmed:meshHeading | pubmed-meshheading:12501184... | lld:pubmed |
| pubmed-article:12501184 | pubmed:meshHeading | pubmed-meshheading:12501184... | lld:pubmed |
| pubmed-article:12501184 | pubmed:meshHeading | pubmed-meshheading:12501184... | lld:pubmed |
| pubmed-article:12501184 | pubmed:meshHeading | pubmed-meshheading:12501184... | lld:pubmed |
| pubmed-article:12501184 | pubmed:meshHeading | pubmed-meshheading:12501184... | lld:pubmed |
| pubmed-article:12501184 | pubmed:meshHeading | pubmed-meshheading:12501184... | lld:pubmed |
| pubmed-article:12501184 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12501184 | pubmed:articleTitle | Biochemical and structural characterization of the cross-linked complex of nitrogenase: comparison to the ADP-AlF4(-)-stabilized structure. | lld:pubmed |
| pubmed-article:12501184 | pubmed:affiliation | Division of Chemistry and Chemical Engineering 114-96, California Institute of Technology, Pasadena, CA 91125, USA. | lld:pubmed |
| pubmed-article:12501184 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12501184 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12501184 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:12501184 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12501184 | lld:pubmed |
