Alternate quinone coupling in a new class of succinate dehydrogenase may potentiate mycobacterial respiratory control.

Abstract:

:There is a paucity of information on the unique components that pathogens use to form respiratory chains. It is not known why mycobacteria encode multiple succinate dehydrogenases (SDHs) to perform menaquinone-linked succinate oxidation, a thermodynamically unfavorable reaction (ΔG° = +21 kJ·mol-1 ). In other bacteria, specific di-heme SDHs overcome this using the proton motive force. It is unknown if this holds true in mycobacteria. Here, succinate dehydrogenase 1 (Sdh1) from Mycobacterium smegmatis was purified and found to not contain heme cofactors. Proteoliposomes, containing Sdh1, are active with coenzyme Q2 (Km  ~ 12 μm), are competitively inhibited by menaquinone (Ki  ~ 25 μm) and do not generate or consume electrochemical gradients. Sdh1 may use higher potential quinones in vivo and forms a novel SDH class, which we term 'Type F'.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Hards K,Rodriguez SM,Cairns C,Cook GM

doi

10.1002/1873-3468.13330

subject

Has Abstract

pub_date

2019-03-01 00:00:00

pages

475-486

issue

5

eissn

0014-5793

issn

1873-3468

journal_volume

593

pub_type

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