The structure and reactivity of the HoxEFU complex from the cyanobacterium Synechocystis sp. PCC 6803

Artz, Jacob H.; Tokmina-Lukaszewska, Monika; Mulder, David W.; Lubner, Carolyn E.; Gutekunst, Kirstin; Appel, Jens; Bothner, Brian; Boehm, Marko; King, Paul W.

doi:10.1074/jbc.RA120.013136

Title: The structure and reactivity of the HoxEFU complex from the cyanobacterium Synechocystis sp. PCC 6803

Journal Article · Wed Jul 01 00:00:00 EDT 2020 · Journal of Biological Chemistry

DOI:https://doi.org/10.1074/jbc.RA120.013136· OSTI ID:1769484

Artz, Jacob H.; Tokmina-Lukaszewska, Monika; Mulder, David W.; Lubner, Carolyn E.;

; Appel, Jens; Bothner, Brian; Boehm, Marko;

Cyanobacterial Hox is a [NiFe] hydrogenase that consists of the hydrogen (H₂)-activating subunits HoxYH, which form a complex with the HoxEFU assembly to mediate reactions with soluble electron carriers like NAD(P)H and ferredoxin (Fdx), thereby coupling photosynthetic electron transfer to energy-transforming catalytic reactions. Researchers studying the HoxEFUYH complex have observed that HoxEFU can be isolated independently of HoxYH, leading to the hypothesis that HoxEFU is a distinct functional subcomplex rather than an artifact of Hox complex isolation. Moreover, outstanding questions about the reactivity of Hox with natural substrates and the site(s) of substrate interactions and coupling of H₂, NAD(P)H, and Fdx remain to be resolved. To address these questions, here we analyzed recombinantly produced HoxEFU by electron paramagnetic resonance spectroscopy and kinetic assays with natural substrates. The purified HoxEFU subcomplex catalyzed electron transfer reactions among NAD(P)H, flavodoxin, and several ferredoxins, thus functioning in vitro as a shuttle among different cyanobacterial pools of reducing equivalents. Both Fdx1-dependent reductions of NAD⁺ and NADP⁺ were cooperative. HoxEFU also catalyzed the flavodoxin-dependent reduction of NAD(P)⁺, Fdx2-dependent oxidation of NADH and Fdx4- and Fdx11-dependent reduction of NAD⁺. MS-based mapping identified an Fdx1-binding site at the junction of HoxE and HoxF, adjacent to iron-sulfur (FeS) clusters in both subunits. Overall, the reactivity of HoxEFU observed here suggests that it functions in managing peripheral electron flow from photosynthetic electron transfer, findings that reveal detailed insights into how ubiquitous cellular components may be used to allocate energy flow into specific bioenergetic products.

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Research Organization:: National Renewable Energy Laboratory (NREL), Golden, CO (United States)

Sponsoring Organization:: USDOE; USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences & Biosciences Division; National Institutes of Health (NIH)

Grant/Contract Number:: AC36-08GO28308; P20GM103474

OSTI ID:: 1769484

Alternate ID(s):: OSTI ID: 1659972

Report Number(s):: NREL/JA-2700-76164; S0021925817489654; PII: S0021925817489654

Journal Information:: Journal of Biological Chemistry, Journal Name: Journal of Biological Chemistry Vol. 295 Journal Issue: 28; ISSN 0021-9258

Publisher:: ElsevierCopyright Statement

Country of Publication:: United States

Language:: English

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59 BASIC BIOLOGICAL SCIENCES
bidirectional hydrogenase
diaphorase
electron paramagnetic resonance (EPR)
HoxEFU
kinetics
nickel-iron enzyme
photosynthesis
protein cross-linking
protein-protein interaction
Synechocystis

Title: The structure and reactivity of the HoxEFU complex from the cyanobacterium Synechocystis sp. PCC 6803

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