YhjA - An Escherichia coli trihemic enzyme with quinol peroxidase activity
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چکیده
منابع مشابه
Cytochrome bd Displays Significant Quinol Peroxidase Activity
Cytochrome bd is a prokaryotic terminal oxidase that catalyses the electrogenic reduction of oxygen to water using ubiquinol as electron donor. Cytochrome bd is a tri-haem integral membrane enzyme carrying a low-spin haem b558, and two high-spin haems: b595 and d. Here we show that besides its oxidase activity, cytochrome bd from Escherichia coli is a genuine quinol peroxidase (QPO) that reduce...
متن کاملThe Escherichia coli yhjA gene, encoding a predicted cytochrome c peroxidase, is regulated by FNR and OxyR.
The Escherichia coli FNR protein is an oxygen-responsive global transcription factor, and OxyR is a key regulator of the peroxide stress response. Here both FNR and OxyR are shown to regulate expression of the E. coli yhjA gene. The yhjA gene encodes a predicted cytochrome c peroxidase, a bacterial haem-containing protein involved in the peroxide stress response through its ability to convert h...
متن کاملCrystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site.
The quinol-fumarate reductase (QFR) respiratory complex of Escherichia coli is a four-subunit integral-membrane complex that catalyzes the final step of anaerobic respiration when fumarate is the terminal electron acceptor. The membrane-soluble redox-active molecule menaquinol (MQH(2)) transfers electrons to QFR by binding directly to the membrane-spanning region. The crystal structure of QFR c...
متن کاملReversible synthesis of polyribonucleotides with an enzyme from Escherichia coli.
Studies on nucleotide and coenzyme synthesis in this laboratory led to an attempt to convert nucleoside 5’-polyphosphates to polyribonucleotides. We were able to show that extracts of Escherichia coli convert C14-adenine-labeled ATP1 to an acid-insoluble nucleotide, and that the addition of adenylate kinase increased the rate of the reaction (1, 2). The discovery of Ochoa and coworkers ( 3 , 4)...
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malQ mutants of Escherichia coli lacking amylomaltase cannot grow on maltose. They express the maltose system constitutively and are sensitive to maltose when grown on another carbon source. In an attempt to isolate a multicopy suppressor that would result in growth on maltose, we transformed a malQ mutant with a gene bank of E. coli DNA which had been digested with Sau3a and cloned in pBR322. ...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Bioenergetics
سال: 2018
ISSN: 0005-2728
DOI: 10.1016/j.bbabio.2018.03.008