The Catalytic Power of Magnesium Chelatase: a Benchmark for the AAA(+) ATPases

Overview

Journal FEBS Lett

Specialty Biochemistry

Date 2016 May 14

PMID 27176620

Citations 8

Authors

Nathan B P Adams

Amanda A Brindley

C Neil Hunter

James D Reid

Affiliations

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Abstract

In the first committed reaction of chlorophyll biosynthesis, magnesium chelatase couples ATP hydrolysis to the thermodynamically unfavorable Mg(2+) insertion into protoporphyrin IX (ΔG°' of circa 25-33 kJ·mol(-1) ). We explored the thermodynamic constraints on magnesium chelatase and demonstrate the effect of nucleotide hydrolysis on both the reaction kinetics and thermodynamics. The enzyme produces a significant rate enhancement (kcat /kuncat of 400 × 10(6) m) and a catalytic rate enhancement, kcat/KmDIXK0.5Mgkuncat, of 30 × 10(15) m(-1) , increasing to 300 × 10(15) m(-1) with the activator protein Gun4. This is the first demonstration of the thermodynamic benefit of ATP hydrolysis in the AAA(+) family.

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