A structure-function analysis of chlorophyllase reveals a mechanism for activity regulation dependent on disulfide bonds

Jo, Minshik; Knapp, Madison; Boggs, David G.; Brimberry, Marley; Donnan, Patrick H.; Bridwell-Rabb, Jennifer

doi:10.1016/j.jbc.2023.102958

A structure-function analysis of chlorophyllase reveals a mechanism for activity regulation dependent on disulfide bonds

Journal Article · Tue Feb 28 00:00:00 EST 2023 · Journal of Biological Chemistry

DOI:https://doi.org/10.1016/j.jbc.2023.102958· OSTI ID:1923104

^[1]; ^[1]; ^[1]; Brimberry, Marley ^[1]; ^[1]; Bridwell-Rabb, Jennifer ^[1]

University of Michigan, Ann Arbor, MI (United States)

Chlorophyll pigments are used by photosynthetic organisms to facilitate light capture and mediate the conversion of sunlight into chemical energy. Due to the indispensable nature of this pigment and its propensity to form reactive oxygen species, organisms heavily invest in its biosynthesis, recycling, and degradation. One key enzyme implicated in these processes is chlorophyllase, an α/β hydrolase that hydrolyzes the phytol tail of chlorophyll pigments to produce chlorophyllide molecules. This enzyme was discovered a century ago, but despite its importance to diverse photosynthetic organisms, there are still many missing biochemical details regarding how chlorophyllase functions. Here, we present the 4.46-Å resolution crystal structure of chlorophyllase from Triticum aestivum. This structure reveals the dimeric architecture of chlorophyllase, the arrangement of catalytic residues, an unexpected divalent metal ion–binding site, and a substrate-binding site that can accommodate a diverse range of pigments. Further, this structure exhibits the existence of both intermolecular and intramolecular disulfide bonds. We investigated the importance of these architectural features using enzyme kinetics, mass spectrometry, and thermal shift assays. Through this work, we demonstrated that the oxidation state of the Cys residues is imperative to the activity and stability of chlorophyllase, illuminating a biochemical trigger for responding to environmental stress. Additional bioinformatics analysis of the chlorophyllase enzyme family reveals widespread conservation of key catalytic residues and the identified “redox switch” among other plant chlorophyllase homologs, thus revealing key details regarding the structure-function relationships in chlorophyllase.

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Research Organization:: Univ. of Michigan, Ann Arbor, MI (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES). Scientific User Facilities (SUF); Michigan Technology Tri-Corridor; USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: SC0021240; AC02-06CH11357; 085P1000817

OSTI ID:: 1923104

Alternate ID(s):: OSTI ID: 1975395

Journal Information:: Journal of Biological Chemistry, Vol. 299, Issue 3; ISSN 0021-9258

Publisher:: American Society for Biochemistry and Molecular BiologyCopyright Statement

Country of Publication:: United States

Language:: English

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A structure-function analysis of chlorophyllase reveals a mechanism for activity regulation dependent on disulfide bonds

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