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24:
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409:, and binds at the quinol oxidation (Qo) site of the bc1 complex, blocking electron transfer to the Rieske iron-sulfur protein. Binding of myxothiazol induces a red-shift to the visible absorption spectrum of reduced haem bl. In contrast to
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InChI=1S/C25H33N3O3S2/c1-16(2)9-7-8-10-17(3)24-28-20(15-33-24)25-27-19(14-32-25)11-12-21(30-5)18(4)22(31-6)13-23(26)29/h7-18,21H,1-6H3,(H2,26,29)/b9-7+,10-8+,12-11+,22-13+/t17?,18-,21+/m1/s1
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Gebhard von Jagow, W. D. Engel (1981). "Complete
Inhibition of Electron Transfer from Ubiquinol to Cytochrome by the Combined Action of Antimycin and Myxothiazol".
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to the Rieske iron-sulfur protein, binding instead in the 'b-proximal' region of the
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Except where otherwise noted, data are given for materials in their
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C((/C=C/c1csc(n1)c2csc(n2)C(C)/C=C/C=C/C(C)C)OC)/C(=C\C(=O)N)/OC
444:"Myxothiazol, a new antibiotic interfering with respiration"
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is therefore unaffected by the binding of this inhibitor.
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421:Qo site. Movement of the cytoplasmic domain of the
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442:Georg Thierbach, Hans Reichenbach (1981).
405:Myxothiazol is a competitive inhibitor of
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383:is a chemical compound produced by the
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449:Antimicrobial Agents and Chemotherapy
248:Key: XKTFQMCPGMTBMD-YCSHSZEBSA-N
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400:coenzyme Q - cytochrome c reductase
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14:
42:-4-yl}-3,5-dimethoxy-4-methyl- (2
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342:(at 25 °C , 100 kPa).
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394:of the mitochondrial
462:10.1128/AAC.19.4.504
58:)-2,6-heptadienamide
332: g·mol
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369:Infobox references
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537:Enzyme inhibitors
388:Myxococcus fulvus
377:Chemical compound
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105:Interactive image
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456:(4): 504–507.
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503:(1): 19–24.
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496:FEBS Letters
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411:stigmatellin
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390:. It is an
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64:Identifiers
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17:Myxothiazol
381:Myxothiazol
278:Properties
181:Myxothiazol
163:100.151.224
125:CHEBI:25461
531:Categories
429:References
325:Molar mass
223:6VY98BQ7NB
136:ChemSpider
92:3D model (
81:76706-55-3
71:CAS Number
37:IUPAC name
542:Thiazoles
407:ubiquinol
398:complex (
392:inhibitor
517:7319059
480:7247372
362:what is
360: (
203:6437357
190:PubChem
145:4941921
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478:
471:181466
468:
357:verify
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330:487.68
262:SMILES
40:7-{2'-
31:Names
237:InChI
116:ChEBI
94:JSmol
513:PMID
476:PMID
214:UNII
175:MeSH
505:doi
501:136
466:PMC
458:doi
402:).
193:CID
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454:19
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300:33
294:25
54:,6
50:,5
46:,4
519:.
507::
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460::
352:Y
318:2
315:S
312:3
309:O
306:3
303:N
297:H
291:C
96:)
56:E
52:S
48:R
44:E
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