DC Field | Value | Language |
---|---|---|
dc.contributor.author | Houseman, ALP | ko |
dc.contributor.author | Oh, Byung-Ha | ko |
dc.contributor.author | Kennedy, MC | ko |
dc.contributor.author | Fan, CL | ko |
dc.contributor.author | Werst, MM | ko |
dc.contributor.author | Beinert, H | ko |
dc.contributor.author | Markley, JL | ko |
dc.contributor.author | Hoffman, BM | ko |
dc.date.accessioned | 2013-02-24T08:35:27Z | - |
dc.date.available | 2013-02-24T08:35:27Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 1992-02 | - |
dc.identifier.citation | BIOCHEMISTRY, v.31, no.7, pp.2073 - 2080 | - |
dc.identifier.issn | 0006-2960 | - |
dc.identifier.uri | http://hdl.handle.net/10203/55756 | - |
dc.description.abstract | The benefits of performing ENDOR experiments at higher microwave frequency are demonstrated in a Q-band (35 GHz) ENDOR investigation of a number of proteins with [nFe-mS] clusters, n = 2, 3, 4. Each protein displays several resonances in the frequency range of 0-20 MHz. In all instances, features are seen near nu almost-equal-to 13 and 8 MHz that can be assigned, respectively, to "distant ENDOR' from C-13 in natural-abundance (1.1%) and from N-14 (the DELTA-m(I) = +/- 2 transitions); the nuclei involved in this phenomenon are remote from and have negligible hyperfine couplings to the cluster. In addition, a number of proteins show local C-13 ENDOR signals with resolved hyperfine interactions; these are assigned to the beta-carbons of cysteines bound to the cluster [A(C-13) almost-equal-to 1.0 MHz]. Five proteins show resolved, local DELTA-m1 = +/- 2 ENDOR signals from N-14 with an isotropic hyperfine coupling, 0.4 less than or similar to A(N-14) less than or similar to 1.0, similar to those seen in ESEEM studies; these most likely are associated with N-H...S hydrogen bonds to the cluster. Anabaena ferredoxin further shows a signal corresponding to A(N-14) almost-equal-to 4 MHz. Quadrupole coupling constants are derived for both local and distant N-14 signals. The interpretation of the data is supported by studies on N-15- and C-13-enriched ferredoxin (Fd) from Anabaena 7120, where the N-15 signals can be clearly correlated with the corresponding N-14 signals and where the C-13 Signals are strongly enhanced. Thus, the observation of N-14 DELTA-m(I) = +/- 2 signals at Q-band provides a new technique for examining weak interactions with a cluster. Six proteins show an additional pattern near nu almost-equal-to 18 MHz that arises from Fe-57 in natural abundance (2.2%) with A(Fe-57) almost-equal-to 36 MHz, which opens the possibility of studying proteins for which enrichment is impractical. Q-band ENDOR studies also have been carried out on four H-2-exchanged Fe-S proteins, and ENDOR detects exchangeable protons in each. The importance of these findings for the interpretation of X- and Q-band ENDOR at low radiofrequencies is discussed. | - |
dc.language | English | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.subject | NUCLEAR DOUBLE-RESONANCE | - |
dc.subject | CLOSTRIDIUM-PASTEURIANUM | - |
dc.subject | ACONITASE | - |
dc.subject | IRON | - |
dc.subject | SPECTROSCOPY | - |
dc.subject | POLARIZATION | - |
dc.subject | HYDROGENASE | - |
dc.subject | FERREDOXIN | - |
dc.subject | REDUCTASE | - |
dc.subject | CRYSTAL | - |
dc.title | 14,15N, 13C, 57Fe, and 1,2H Q-band ENDOR study of Fe-S proteins with clusters that have endogenous sulfur ligands | - |
dc.type | Article | - |
dc.identifier.wosid | A1992HF26700026 | - |
dc.identifier.scopusid | 2-s2.0-0026609797 | - |
dc.type.rims | ART | - |
dc.citation.volume | 31 | - |
dc.citation.issue | 7 | - |
dc.citation.beginningpage | 2073 | - |
dc.citation.endingpage | 2080 | - |
dc.citation.publicationname | BIOCHEMISTRY | - |
dc.identifier.doi | 10.1021/bi00122a026 | - |
dc.contributor.localauthor | Oh, Byung-Ha | - |
dc.contributor.nonIdAuthor | Houseman, ALP | - |
dc.contributor.nonIdAuthor | Kennedy, MC | - |
dc.contributor.nonIdAuthor | Fan, CL | - |
dc.contributor.nonIdAuthor | Werst, MM | - |
dc.contributor.nonIdAuthor | Beinert, H | - |
dc.contributor.nonIdAuthor | Markley, JL | - |
dc.contributor.nonIdAuthor | Hoffman, BM | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | NUCLEAR DOUBLE-RESONANCE | - |
dc.subject.keywordPlus | CLOSTRIDIUM-PASTEURIANUM | - |
dc.subject.keywordPlus | ACONITASE | - |
dc.subject.keywordPlus | IRON | - |
dc.subject.keywordPlus | SPECTROSCOPY | - |
dc.subject.keywordPlus | POLARIZATION | - |
dc.subject.keywordPlus | HYDROGENASE | - |
dc.subject.keywordPlus | FERREDOXIN | - |
dc.subject.keywordPlus | REDUCTASE | - |
dc.subject.keywordPlus | CRYSTAL | - |
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