Converting a cysteine-rich natively noncatalytic protein to an artificial hydrogenase.

Malayam Parambath, Sreya; Prakash, Divyansh; Swetman, Windfield; Surakanti, Aditya; Chakraborty, Saumen

Malayam Parambath, Sreya; Prakash, Divyansh; Swetman, Windfield; Surakanti, Aditya; Chakraborty, Saumen.

Afiliación

Malayam Parambath S; Department of Chemistry and Biochemistry, University of Mississippi, University, MS 38677, USA. saumenc@olemiss.edu.
Prakash D; Department of Chemistry and Biochemistry, University of Mississippi, University, MS 38677, USA. saumenc@olemiss.edu.
Swetman W; Department of Chemistry and Biochemistry, University of Mississippi, University, MS 38677, USA. saumenc@olemiss.edu.
Surakanti A; Department of Chemistry and Biochemistry, University of Mississippi, University, MS 38677, USA. saumenc@olemiss.edu.
Chakraborty S; Department of Chemistry and Biochemistry, University of Mississippi, University, MS 38677, USA. saumenc@olemiss.edu.

Chem Commun (Camb) ; 59(89): 13325-13328, 2023 Nov 07.

Article en En | MEDLINE | ID: mdl-37867329

RESUMEN

An artificial hydrogenase is constructed when the natively noncatalytic α-domain of the Cys-rich protein metallothionein (MT) is assembled with NiII. αMT binds four eq. of NiII in a non-cooperative manner where the addition of the 1st NiII eq. affords the most catalytically active species with little effect on photocatalytic H2 production during subsequent metal addition. The critical role of protonated Cys residue(s) in H-H bond formation is demonstrated.

Asunto(s)

Hidrogenasas; Hidrogenasas/química; Cisteína/química

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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Hidrogenasas Idioma: En Revista: Chem Commun (Camb) Asunto de la revista: QUIMICA Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido

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