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粗糙脉孢菌中对氰化物和异羟肟酸耐药的呼吸作用

Cyanide- and hydroxamate-resistant respiration in Neurospora crassa.

作者信息

Edwards D L, Unger B W

出版信息

J Bacteriol. 1978 Mar;133(3):1130-4. doi: 10.1128/jb.133.3.1130-1134.1978.

Abstract

Strain inl-89601 of Neurospora crassa respires exclusively by means of the mitochondrial cytochrome chain. The respiration of this strain is entirely inhibited by cyanide or antimycin A, the classical inhibitors of cytochrome chain respiration. When this strain was grown in the presence of chloramphenicol, however, two additional terminal oxidases were detected. One of these oxidases is inhibited by substituted hydroxamic acids and has been described previously. The second oxidase was not inhibited by cyanide or hydroxamic acid but was inhibited by azide in the presence of both cyanide and hydroxamic acid. This azide-sensitive respiration was due to a single respiratory pathway with a Ki for azide of 200 micrometer. A small amount of azide-sensitive respiration was detected in mitochondrial fractions obtained from chloramphenicol-treated cells, and it is likely that the azide-sensitive oxidase is localized in the mitochondrion. The determinants for the azide-sensitive and hydroxamate-sensitive oxidases segregate in a Mendelian manner in crosses and are either unlinked or not closely linked to each other.

摘要

粗糙脉孢菌菌株inl - 89601仅通过线粒体细胞色素链进行呼吸。该菌株的呼吸完全被氰化物或抗霉素A抑制,这两种物质是细胞色素链呼吸的经典抑制剂。然而,当该菌株在氯霉素存在的情况下生长时,检测到另外两种末端氧化酶。其中一种氧化酶被取代异羟肟酸抑制,并且之前已有描述。第二种氧化酶不受氰化物或异羟肟酸抑制,但在氰化物和异羟肟酸同时存在的情况下被叠氮化物抑制。这种对叠氮化物敏感的呼吸是由于单一的呼吸途径,其对叠氮化物的Ki为200微摩尔。在从氯霉素处理的细胞中获得的线粒体组分中检测到少量对叠氮化物敏感的呼吸,并且对叠氮化物敏感的氧化酶可能定位于线粒体中。在杂交中,对叠氮化物敏感和对异羟肟酸敏感的氧化酶的决定因素以孟德尔方式分离,并且彼此不连锁或紧密连锁。

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本文引用的文献

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Selection of respiratory mutants of Neurospora crassa.粗糙脉孢菌呼吸突变体的筛选。
J Bacteriol. 1973 Apr;114(1):164-8. doi: 10.1128/jb.114.1.164-168.1973.
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Cyanide-resistant respiration in Neurospora crassa.粗糙脉孢菌中的抗氰呼吸。
J Bacteriol. 1971 Dec;108(3):1087-96. doi: 10.1128/jb.108.3.1087-1096.1971.
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Regulation of cyanide-insensitive respiration in Neurospora.粗糙脉孢菌中氰化物不敏感呼吸的调控
Eur J Biochem. 1976 Feb 16;62(2):217-21. doi: 10.1111/j.1432-1033.1976.tb10150.x.

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