CO as a substrate and inhibitor of H+ reduction for the Mo-, V-, and Fe-nitrogenase isozymes

Harris, Derek F.; Jimenez-Vicente, Emilio; Yang, Zhi-Yong; Hoffman, Brian M.; Dean, Dennis R.; Seefeldt, Lance C.

doi:10.1016/j.jinorgbio.2020.111278

CO as a substrate and inhibitor of H⁺ reduction for the Mo-, V-, and Fe-nitrogenase isozymes

Journal Article · Tue Oct 06 00:00:00 EDT 2020 · Journal of Inorganic Biochemistry

DOI:https://doi.org/10.1016/j.jinorgbio.2020.111278· OSTI ID:1837049

Harris, Derek F. ^[1]; Jimenez-Vicente, Emilio ^[2]; Yang, Zhi-Yong ^[3]; Hoffman, Brian M. ^[3]; Dean, Dennis R. ^[2]; Seefeldt, Lance C. ^[3]

Northwestern Univ., Evanston, IL (United States); Northwestern University
Virginia Polytechnic Inst. and State Univ. (Virginia Tech), Blacksburg, VA (United States)
Northwestern Univ., Evanston, IL (United States)

Three known nitrogenase isozymes, Mo-, V-, and Fe-, catalyze biological reduction of dinitrogen (N₂) to ammonia (NH₃). All three utilize the same reductive elimination mechanism: an intermediate with two metal-bound hydrides reductively-eliminates hydrogen gas (H₂) in a reaction coupled to binding and activation of N₂. Nonetheless, the three isozymes show dramatically different relative rates of H₂ formation and N₂ reduction, revealing important differences in reactivity with substrates. Carbon monoxide (CO) has been characterized as both an inhibitor and substrate for Mo- and V-nitrogenases, but not for the Fe-nitrogenase. In this work, we present a comparative study of the reactivity of the three isozymes with CO, examining CO both as a substrate and as an inhibitor of proton (H⁺) reduction under steady-state conditions. For Mo-nitrogenase, there is neither detectable reduction of CO nor inhibition of H⁺ reduction. Fe- and V-nitrogenase show CO reduction and inhibition of H⁺ reduction that depends on the CO partial pressure. For V-nitrogenase, ethylene (C₂H₄) is the major reduction product with a maximum specific activity of ~7.5 nmol C₂H₄/nmol VFe protein/min at 1 atm CO. The major product of CO reduction for Fe-nitrogenase is methane (CH₄) with a maximum specific activity of ~4.8 nmol CH₄/nmol FeFe protein/min at 0.05 atm CO. The rate of CH₄ production by Fe-nitrogenase progressively increases to a maximum at 0.05 atm CO and then declines to ~10% with increasing CO partial pressure up to 1 atm. CO does not inhibit proton reduction in Mo-nitrogenase but shows 16% inhibition for V-nitrogenase and 35% for Fe-nitrogenase.

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Research Organization:: Northwestern Univ., Evanston, IL (United States); Utah State Univ., Logan, UT (United States); Virginia Polytechnic Inst. and State Univ. (Virginia Tech), Blacksburg, VA (United States)

Sponsoring Organization:: USDOE; USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: SC0010687; SC0010834; SC0019342

OSTI ID:: 1837049

Alternate ID(s):: OSTI ID: 1776415

Journal Information:: Journal of Inorganic Biochemistry, Journal Name: Journal of Inorganic Biochemistry Vol. 213; ISSN 0162-0134

Publisher:: ElsevierCopyright Statement

Country of Publication:: United States

Language:: English

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carbon monoxide
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nitrogenase
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CO as a substrate and inhibitor of H+ reduction for the Mo-, V-, and Fe-nitrogenase isozymes

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CO as a substrate and inhibitor of H⁺ reduction for the Mo-, V-, and Fe-nitrogenase isozymes