5u8z › Citations

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

Sui X, Weitz AC, Farquhar ER, Badiee M, Banerjee S, von Lintig J, Tochtrop GP, Palczewski K, Hendrich MP, Kiser PD
Biochemistry 56 2836-2852 (2017)
Related entries: 5u8x, 5u8y, 5u90, 5u97

Cited: 16 times
EuropePMC logo PMID: 28493664

Abstract

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.

Articles - 5u8z mentioned but not cited (1)

  1. Structure and Spectroscopy of Alkene-Cleaving Dioxygenases Containing an Atypically Coordinated Non-Heme Iron Center. Sui X, Weitz AC, Farquhar ER, Badiee M, Banerjee S, von Lintig J, Tochtrop GP, Palczewski K, Hendrich MP, Kiser PD. Biochemistry 56 2836-2852 (2017)


Reviews citing this publication (5)

  1. The molecular aspects of absorption and metabolism of carotenoids and retinoids in vertebrates. Widjaja-Adhi MAK, Golczak M. Biochim Biophys Acta Mol Cell Biol Lipids 1865 158571 (2020)
  2. Molecular components affecting ocular carotenoid and retinoid homeostasis. von Lintig J, Moon J, Babino D. Prog Retin Eye Res 80 100864 (2021)
  3. Structural and mechanistic aspects of carotenoid cleavage dioxygenases (CCDs). Daruwalla A, Kiser PD. Biochim Biophys Acta Mol Cell Biol Lipids 1865 158590 (2020)
  4. Retinal pigment epithelium 65 kDa protein (RPE65): An update. Kiser PD. Prog Retin Eye Res 88 101013 (2022)
  5. Evolutionary aspects and enzymology of metazoan carotenoid cleavage oxygenases. Poliakov E, Uppal S, Rogozin IB, Gentleman S, Redmond TM. Biochim Biophys Acta Mol Cell Biol Lipids 1865 158665 (2020)

Articles citing this publication (10)

  1. The Biochemical Basis of Vitamin A Production from the Asymmetric Carotenoid β-Cryptoxanthin. Kelly ME, Ramkumar S, Sun W, Colon Ortiz C, Kiser PD, Golczak M, von Lintig J. ACS Chem Biol 13 2121-2129 (2018)
  2. Structures, Spectroscopic Properties, and Dioxygen Reactivity of 5- and 6-Coordinate Nonheme Iron(II) Complexes: A Combined Enzyme/Model Study of Thiol Dioxygenases. Gordon JB, McGale JP, Prendergast JR, Shirani-Sarmazeh Z, Siegler MA, Jameson GNL, Goldberg DP. J Am Chem Soc 140 14807-14822 (2018)
  3. Structural basis for carotenoid cleavage by an archaeal carotenoid dioxygenase. Daruwalla A, Zhang J, Lee HJ, Khadka N, Farquhar ER, Shi W, von Lintig J, Kiser PD. Proc Natl Acad Sci U S A 117 19914-19925 (2020)
  4. A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state. Rizzolo K, Cohen SE, Weitz AC, López Muñoz MM, Hendrich MP, Drennan CL, Elliott SJ. Nat Commun 10 1101 (2019)
  5. Preparation and characterization of metal-substituted carotenoid cleavage oxygenases. Sui X, Farquhar ER, Hill HE, von Lintig J, Shi W, Kiser PD. J Biol Inorg Chem 23 887-901 (2018)
  6. Evidence for distinct rate-limiting steps in the cleavage of alkenes by carotenoid cleavage dioxygenases. Khadka N, Farquhar ER, Hill HE, Shi W, von Lintig J, Kiser PD. J Biol Chem 294 10596-10606 (2019)
  7. Identification of functionally important residues and structural features in a bacterial lignostilbene dioxygenase. Kuatsjah E, Verstraete MM, Kobylarz MJ, Liu AKN, Murphy MEP, Eltis LD. J Biol Chem 294 12911-12920 (2019)
  8. Biochemical and structural characterization of a sphingomonad diarylpropane lyase for cofactorless deformylation. Kuatsjah E, Zahn M, Chen X, Kato R, Hinchen DJ, Konev MO, Katahira R, Orr C, Wagner A, Zou Y, Haugen SJ, Ramirez KJ, Michener JK, Pickford AR, Kamimura N, Masai E, Houk KN, McGeehan JE, Beckham GT. Proc Natl Acad Sci U S A 120 e2212246120 (2023)
  9. Mechanistic Insights into a Stibene Cleavage Oxygenase NOV1 from Quantum Mechanical/Molecular Mechanical Calculations. Lu J, Lai W. ChemistryOpen 8 228-235 (2019)
  10. Structural and functional analysis of lignostilbene dioxygenases from Sphingobium sp. SYK-6. Kuatsjah E, Chan ACK, Katahira R, Haugen SJ, Beckham GT, Murphy MEP, Eltis LD. J Biol Chem 296 100758 (2021)


Quick links