Structure of antimycin A1, a specific electron transfer inhibitor of ubiquinol-cytochrome c oxidoreductase [6]

Journal of the American Chemical Society

Volumn 121, Issue 20, 1999, Pages 4902-4903

  Kim, Hoeon ^a   Esser, Lothar ^a   Hossain, M Bilayet ^b   Xia, Di ^a   Yu, Chang An ^d   Rizo, Josep ^c   Van Der Helm, Dick ^b   Deisenhofer, Johann ^a  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^b UNIVERSITY OF OKLAHOMA   (United States)

^c UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^d OKLAHOMA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMYCIN A1; UBIQUINOL CYTOCHROME C REDUCTASE; UBIQUINOL CYTOCHROME C REDUCTASE INHIBITOR; UNCLASSIFIED DRUG;

CRYSTAL STRUCTURE; ELECTRON TRANSPORT; ENZYME INHIBITION; GEOMETRY; LETTER; MOLECULAR INTERACTION; NONHUMAN; PHOTOSYNTHESIS; PROTEIN CONFORMATION; THREE DIMENSIONAL IMAGING;

EID: 0033606283     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja990190h     Document Type: Letter

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14. NMR experiments were performed on a Varian Unity 500 spectrometer at 25 °C using a 70 mM sample of antimycin A1 dissolved in perdeuterated methanol. The spectral width in all proton dimensions was 4200 Hz. The DQF-COSY spectrum consisted of 400 complex increments (4096 complex points each), with 16 scans per increment. For HSQC and HMBC spectra, the spectral width in the 13C dimension was 10 000 Hz, and 180 complex increments of 2048 complex points each were acquired (32 and 64 scans per increment for HSQC and HMC, respectively).
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