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Cross-link formation of the cysteine 228-tyrosine 272 catalytic cofactor of galactose oxidase does not require dioxygen.

Rogers MS, Hurtado-Guerrero R, Firbank SJ, Halcrow MA, Dooley DM, Phillips SE, Knowles PF, McPherson MJ
Biochemistry 47 10428-39 (2008)
Cited: 25 times
EuropePMC logo PMID: 18771294

Abstract

Galactose oxidase (GO) belongs to a class of proteins that self-catalyze assembly of their redox-active cofactors from active site amino acids. Generation of enzymatically active GO appears to require at least four sequential post-translational modifications: cleavage of a secretion signal sequence, copper-dependent cleavage of an N-terminal pro sequence, copper-dependent formation of a C228-Y272 thioether bond, and generation of the Y272 radical. The last two processes were investigated using a truncated protein (termed premat-GO) lacking the pro sequence and purified under copper-free conditions. Reactions of premat-GO with Cu(II) were investigated using optical, EPR, and resonance Raman spectroscopy, SDS-PAGE, and X-ray crystallography. Premat-GO reacted anaerobically with excess Cu(II) to efficiently form the thioether bond but not the Y272 radical. A potential C228-copper coordinated intermediate (lambda max = 406 nm) in the processing reaction, which had not yet formed the C228-Y272 cross-link, was identified from the absorption spectrum. A copper-thiolate protein complex, with copper coordinated to C228, H496, and H581, was also observed in a 3 min anaerobic soak by X-ray crystallography, whereas a 24 h soak revealed the C228-Y272 thioether bond. In solution, addition of oxygenated buffer to premat-GO preincubated with excess Cu(II) generated the Y272 radical state. On the basis of these data, a mechanism for the formation of the C228-Y272 bond and tyrosyl radical generation is proposed. The 406 nm complex is demonstrated to be a catalytically competent processing intermediate under anaerobic conditions. We propose a potential mechanism which is in common with aerobic processing by Cu(II) until the step at which the second electron acceptor is required.

Reviews - 2vz3 mentioned but not cited (1)

  1. Copper active sites in biology. Solomon EI, Heppner DE, Johnston EM, Ginsbach JW, Cirera J, Qayyum M, Kieber-Emmons MT, Kjaergaard CH, Hadt RG, Tian L. Chem. Rev. 114 3659-3853 (2014)

Articles - 2vz3 mentioned but not cited (1)

  1. Cross-link formation of the cysteine 228-tyrosine 272 catalytic cofactor of galactose oxidase does not require dioxygen. Rogers MS, Hurtado-Guerrero R, Firbank SJ, Halcrow MA, Dooley DM, Phillips SE, Knowles PF, McPherson MJ. Biochemistry 47 10428-10439 (2008)


Reviews citing this publication (5)

  1. Thiol dioxygenases: unique families of cupin proteins. Stipanuk MH, Simmons CR, Karplus PA, Dominy JE. Amino Acids 41 91-102 (2011)
  2. Metalloprotein design using genetic code expansion. Hu C, Chan SI, Sawyer EB, Yu Y, Wang J. Chem Soc Rev 43 6498-6510 (2014)
  3. Activation of dioxygen by copper metalloproteins and insights from model complexes. Quist DA, Diaz DE, Liu JJ, Karlin KD. J. Biol. Inorg. Chem. 22 253-288 (2017)
  4. Exploring oxidative modifications of tyrosine: an update on mechanisms of formation, advances in analysis and biological consequences. Houée-Lévin C, Bobrowski K, Horakova L, Karademir B, Schöneich C, Davies MJ, Spickett CM. Free Radic. Res. 49 347-373 (2015)
  5. π-π Stacking Interaction of Metal Phenoxyl Radical Complexes. Oshita H, Shimazaki Y. Molecules 27 1135 (2022)

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  1. Proteomic mapping of mitochondria in living cells via spatially restricted enzymatic tagging. Rhee HW, Zou P, Udeshi ND, Martell JD, Mootha VK, Carr SA, Ting AY. Science 339 1328-1331 (2013)
  2. Spatially resolved proteomic mapping in living cells with the engineered peroxidase APEX2. Hung V, Udeshi ND, Lam SS, Loh KH, Cox KJ, Pedram K, Carr SA, Ting AY. Nat Protoc 11 456-475 (2016)
  3. A comparative summary of expression systems for the recombinant production of galactose oxidase. Spadiut O, Olsson L, Brumer H. Microb. Cell Fact. 9 68 (2010)
  4. Structure of the Reduced Copper Active Site in Preprocessed Galactose Oxidase: Ligand Tuning for One-Electron O2 Activation in Cofactor Biogenesis. Cowley RE, Cirera J, Qayyum MF, Rokhsana D, Hedman B, Hodgson KO, Dooley DM, Solomon EI. J. Am. Chem. Soc. 138 13219-13229 (2016)
  5. Identifying proteins that can form tyrosine-cysteine crosslinks. Martinie RJ, Godakumbura PI, Porter EG, Divakaran A, Burkhart BJ, Wertz JT, Benson DE. Metallomics 4 1037-42, 1008 (2012)
  6. Probing the Cys-Tyr Cofactor Biogenesis in Cysteine Dioxygenase by the Genetic Incorporation of Fluorotyrosine. Li J, Koto T, Davis I, Liu A. Biochemistry 58 2218-2227 (2019)
  7. Expression, purification, and characterization of galactose oxidase of Fusarium sambucinum in E. coli. Paukner R, Staudigl P, Choosri W, Haltrich D, Leitner C. Protein Expr. Purif. 108 73-79 (2015)
  8. Shifting redox states of the iron center partitions CDO between crosslink formation or cysteine oxidation. Njeri CW, Ellis HR. Arch. Biochem. Biophys. 558 61-69 (2014)
  9. Protein oxidation involved in Cys-Tyr post-translational modification. Hromada SE, Hilbrands AM, Wolf EM, Ross JL, Hegg TR, Roth AG, Hollowell MT, Anderson CE, Benson DE. J. Inorg. Biochem. 176 168-174 (2017)
  10. Galactose oxidase from Fusarium oxysporum--expression in E. coli and P. pastoris and biochemical characterization. Paukner R, Staudigl P, Choosri W, Sygmund C, Halada P, Haltrich D, Leitner C. PLoS ONE 9 e100116 (2014)
  11. Two Fusarium copper radical oxidases with high activity on aryl alcohols. Cleveland M, Lafond M, Xia FR, Chung R, Mulyk P, Hein JE, Brumer H. Biotechnol Biofuels 14 138 (2021)
  12. Active-Site Engineering Switches Carbohydrate Regiospecificity in a Fungal Copper Radical Oxidase. Mathieu Y, Cleveland ME, Brumer H. ACS Catal 12 10264-10275 (2022)
  13. Aha1 Is an Autonomous Chaperone for SULT1A1. Liu X, Wang Y. Chem Res Toxicol 35 1418-1424 (2022)
  14. Catalytic Promiscuity of Galactose Oxidase: A Mild Synthesis of Nitriles from Alcohols, Air, and Ammonia. Vilím J, Knaus T, Mutti FG. Angew. Chem. Int. Ed. Engl. 57 14240-14244 (2018)
  15. Formation of Monofluorinated Radical Cofactor in Galactose Oxidase through Copper-Mediated C-F Bond Scission. Li J, Davis I, Griffith WP, Liu A. J Am Chem Soc 142 18753-18757 (2020)
  16. Kβ X-ray Emission Spectroscopy as a Probe of Cu(I) Sites: Application to the Cu(I) Site in Preprocessed Galactose Oxidase. Lim H, Baker ML, Cowley RE, Kim S, Bhadra M, Siegler MA, Kroll T, Sokaras D, Weng TC, Biswas DR, Dooley DM, Karlin KD, Hedman B, Hodgson KO, Solomon EI. Inorg Chem 59 16567-16581 (2020)
  17. Proximity Labeling Facilitates Defining the Proteome Neighborhood of Photosystem II Oxygen Evolution Complex in a Model Cyanobacterium. Xiao Z, Huang C, Ge H, Wang Y, Duan X, Wang G, Zheng L, Dong J, Huang X, Zhang Y, An H, Xu W, Wang Y. Mol Cell Proteomics 21 100440 (2022)
  18. The effect of π-π stacking interaction of the indole ring with the coordinated phenoxyl radical in a nickel(ii)-salen type complex. Comparison with the corresponding Cu(ii) complex. Oshita H, Suzuki T, Kawashima K, Abe H, Tani F, Mori S, Yajima T, Shimazaki Y. Dalton Trans 48 12060-12069 (2019)


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