Journal
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume 101, Issue 19, Pages 7201-7212Publisher
SPRINGER
DOI: 10.1007/s00253-017-8454-7
Keywords
M. tuberculosis; Ferredoxin; Rv1786; Cytochrome P450mono-oxygenase redox partner; Ferredoxin reductaseA; Flavoprotein reductaseA
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Funding
- National Natural Science Foundation of China (NSFC) [81273427, 81361138020, 81573475]
- National Mega- project for Innovative Drugs [2014ZX09507-009]
- Beijing Science and Technology Projects [Z141102004414065, Z151100000315029]
- CAMS Initiative Fund for Innovative Medicine [2016-I2M-3-014]
- Peking Union Medical College (PUMC) Youth Fund [33320140177, 3332016139]
- China Scholarship Council (CSC) State-Sponsored Scholarship Program for Visiting Scholars in Sweden/Europe [CSC2014-3012/201408110091-2]
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Ferredoxins are iron-sulfur protein that mediate electron transfer in cytochrome P450 mono-oxygenase (CYP)-related catalytic reactions in a wide variety of organisms. Rv1786 is a putative ferredoxin, encoded by a gene located downstream of the gene encoding CYP143A1 in the Mycobacterium tuberculosis genome. However, the structure and function of Rv1786 have remained unclear. Here, the recombinant Mtb Rv1786 was expressed, purified as a His-tagged form and characterized with [3Fe-4S] clusters as its cofactors using a series of measurements including SDS-PAGE, western blot, UV/Visible, MALDI-TOF/TOF-MS, and electron paramagnetic resonance spectroscopic analysis. Based on the assessments of surface plasmon resonance (SPR) and steady state kinetic assays, Rv1786 was found to be able to couple with both ferredoxin reductase A (FdrA) and flavoprotein reductase A (FprA) as redox partner, but with a stronger binding to FprA and a better coupling activity to FdrA. Preliminary structural and biochemical characterization of Mtb Rv1786 as a redox partner is presented here.
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