An Overview of the Electron-Transfer Proteins That Activate Alkane Monooxygenase (AlkB).

An Overview of the Electron-Transfer Proteins That Activate Alkane Monooxygenase (AlkB).
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DOI:
10.3389/fmicb.2022.845551
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发表时间:
2022
影响因子:
5.2
通讯作者:
Austin RN
Austin RN
中科院分区:
生物学2区
文献类型:
--
作者:
Williams SC;Austin RN

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烷烃氧化酶在全球碳循环中发挥着重要作用。烷烃单加氧酶 (AlkB) 可氧化环境中的大部分中链烷烃。第一个发现的 AlkB 是在 20 世纪 70 年代初从 P. putida GPo1(最初称为 P. oleovorans)中发现的,并且它仍然是最为人所知的家族成员。该 AlkB 是 OCT 操纵子的一部分,其中存在烷烃生长所需的所有关键蛋白。 AlkB 催化循环需要还原二铁活性位点。在恶臭假单胞菌 GPo1 中,电子源自 NADH,并通过黄素还原酶和铁硫蛋白(红氧还蛋白)到达 AlkB。在本次小型综述中,我们将回顾有关激活 AlkB 的电子转移蛋白的规范排列的已知信息,更重要的是,指出其他几种可能的排列。这些其他排列包括存在比规范排列更简单的红氧还蛋白,以及具有融合电子转移伙伴的其他两类 AlkB。在一类中,红氧还蛋白与羟化酶融合,而在另一类尚未充分研究的类别中,铁氧还蛋白还原酶和铁氧还蛋白与羟化酶融合。我们回顾了这些电子转移蛋白的生物化学知识,推测了这种多样性的生物学意义,并指出了未来研究的关键问题。
Alkane-oxidizing enzymes play an important role in the global carbon cycle. Alkane monooxygenase (AlkB) oxidizes most of the medium-chain length alkanes in the environment. The first AlkB identified was from P. putida GPo1 (initially known as P. oleovorans) in the early 1970s, and it continues to be the family member about which the most is known. This AlkB is found as part of the OCT operon, in which all of the key proteins required for growth on alkanes are present. The AlkB catalytic cycle requires that the diiron active site be reduced. In P. putida GPo1, electrons originate from NADH and arrive at AlkB via the intermediacy of a flavin reductase and an iron–sulfur protein (a rubredoxin). In this Mini Review, we will review what is known about the canonical arrangement of electron-transfer proteins that activate AlkB and, more importantly, point to several other arrangements that are possible. These other arrangements include the presence of a simpler rubredoxin than what is found in the canonical arrangement, as well as two other classes of AlkBs with fused electron-transfer partners. In one class, a rubredoxin is fused to the hydroxylase and in another less well-explored class, a ferredoxin reductase and a ferredoxin are fused to the hydroxylase. We review what is known about the biochemistry of these electron-transfer proteins, speculate on the biological significance of this diversity, and point to key questions for future research.
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