Structure and Spectroscopy of Alkene-Cleaving Dioxygenases Containing an Atypically Coordinated Non-Heme Iron Center

Sui, Xuewu; Weitz, Andrew C.; Farquhar, Erik R.; Badiee, Mohsen; Banerjee, Surajit; von Lintig, Johannes; Tochtrop, Gregory P.; Palczewski, Krzysztof; Hendrich, Michael P.; Kiser, Philip D.

doi:10.1021/acs.biochem.7b00251

Title: Structure and Spectroscopy of Alkene-Cleaving Dioxygenases Containing an Atypically Coordinated Non-Heme Iron Center

Journal Article · Thu May 11 00:00:00 EDT 2017 · Biochemistry

DOI:https://doi.org/10.1021/acs.biochem.7b00251· OSTI ID:1376251

Sui, Xuewu ^[1]; Weitz, Andrew C. ^[2]; Farquhar, Erik R. ^[3]; Badiee, Mohsen ^[1]; Banerjee, Surajit ^[4]; von Lintig, Johannes ^[1]; Tochtrop, Gregory P. ^[1];

^[1]; Hendrich, Michael P. ^[2];

^[5]

Case Western Reserve Univ., Cleveland, OH (United States)
Carnegie Mellon Univ., Pittsburgh, PA (United States)
Brookhaven National Lab. (BNL), Upton, NY (United States); Case Western Reserve Univ., Cleveland, OH (United States)
Argonne National Lab. (ANL), Argonne, IL (United States); Cornell Univ., Ithaca, NY (United States)
Case Western Reserve Univ., Cleveland, OH (United States); Louis Stokes Cleveland VA Medical Center, Cleveland, OH (United States)

Carotenoid cleavage oxygenases (CCOs) are non-heme iron enzymes that catalyze scission of alkene groups in carotenoids and stilbenoids to form biologically important products. CCOs possess a rare four-His iron center whose resting-state structure and interaction with substrates are incompletely understood. Here, we address this knowledge gap through a comprehensive structural and spectroscopic study of three phyletically diverse CCOs. The crystal structure of a fungal stilbenoid-cleaving CCO, CAO1, reveals strong similarity between its iron center and those of carotenoid-cleaving CCOs, but with a markedly different substrate-binding cleft. These enzymes all possess a five-coordinate high-spin Fe(II) center with resting-state Fe–His bond lengths of ~2.15 Å. This ligand set generates an iron environment more electropositive than those of other non-heme iron dioxygenases as observed by Mössbauer isomer shifts. Dioxygen (O₂) does not coordinate iron in the absence of substrate. Substrates bind away (~4.7 Å) from the iron and have little impact on its electronic structure, thus excluding coordination-triggered O₂ binding. However, substrate binding does perturb the spectral properties of CCO Fe–NO derivatives, indicating proximate organic substrate and O₂-binding sites, which might influence Fe–O₂ interactions. Together, these data provide a robust description of the CCO iron center and its interactions with substrates and substrate mimetics that illuminates commonalities as well as subtle and profound structural differences within the CCO family.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES). Scientific User Facilities Division; National Institutes of Health (NIH); Burroughs Wellcome Fund; National Science Foundation (NSF)

Grant/Contract Number:: AC02-98CH10886; AC02-76SF00515; EY009339; EY020551; CA157735; IK2BX002683; CHE1126268; GM103403; RR029205; P30-EB-009998

OSTI ID:: 1376251

Journal Information:: Biochemistry, Vol. 56, Issue 22; ISSN 0006-2960

Publisher:: American Chemical Society (ACS)Copyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 19 works

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Title: Structure and Spectroscopy of Alkene-Cleaving Dioxygenases Containing an Atypically Coordinated Non-Heme Iron Center

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