Structure and quantum chemical characterization of chloroperoxidase compound 0, a common reaction intermediate of diverse heme enzymes

Kühnel, Karin; Derat, Étienne; Terner, James; Shaik, Sason; Schlichting, Ilme

doi:10.1073/pnas.0606285103

Cited by 91 publications

(109 citation statements)

References 56 publications

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“…The average OOO distance in these structures is 1.444 Ϯ 0.058 Å. The recently reported OOO distances of bound peroxide detectable in high-resolution X-ray structures of hemoproteins (determined at Ͻ1.9-Å resolution) are between 1.28 and 1.49 Å (21)(22)(23)). An OOO bond distance of 1.7 Å is thus significantly longer than the length of a typical OOO single bond.…”

Section: Structure and Stability Of The Ligand Bridging The 2 Metals mentioning

confidence: 88%

A peroxide bridge between Fe and Cu ions in the O ₂ reduction site of fully oxidized cytochrome c oxidase could suppress the proton pump

Aoyama

Muramoto

Shinzawa‐Itoh

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

132

152

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For identification of structural differences causing the remarkable functional difference between these 2 distinct fully oxidized forms, the X-ray structure of the fully oxidized as-isolated bovine heart cytochrome c oxidase was determined at 1.95-Å resolution by limiting the X-ray dose for each shot and by using many (Ϸ400) single crystals. This minimizes the effects of hydrated electrons induced by the X-ray irradiation. The X-ray structure showed a peroxide group bridging the 2 metal sites in the O 2 reduction site (Fe 3؉ -O ؊ -O ؊ -Cu 2؉ ), in contrast to a ferric hydroxide (Fe 3؉ -OH ؊ ) in the fully oxidized form immediately after complete oxidation from the fully reduced form, as has been revealed by resonance Raman analyses. The peroxide-bridged structure is consistent with the reductive titration results showing that 6 electron equivalents are required for complete reduction of the fully oxidized as-isolated form. The structural difference between the 2 fully oxidized forms suggests that the bound peroxide in the O 2 reduction site suppresses the proton pumping function.hydrated electron ͉ O2 reduction mechanism ͉ membrane protein ͉ X-ray structural analysis ͉ cell respiration

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Section: Structure and Stability Of The Ligand Bridging The 2 Metals mentioning

confidence: 88%

A peroxide bridge between Fe and Cu ions in the O ₂ reduction site of fully oxidized cytochrome c oxidase could suppress the proton pump

Aoyama

Muramoto

Shinzawa‐Itoh

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

132

152

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“…In another example, reduction of the haem iron by synchrotron radiation followed by transient warming to room temperature was used to generate and trap intermediate states in crystalline myoglobin (Hersleth et al, 2008). Research on other crystalline redox-sensitive proteins for which X-rayinduced reduction has been reported at temperatures close to 100 K (Berglund et al, 2002;Adam et al, 2004;Baxter et al, 2004;Mees et al, 2004;Roberts et al, 2005;Echalier et al, 2006;Beitlich et al, 2007;Kuhnel et al, 2007;Pearson et al, 2007;Hough et al, 2008) could benefit from temperaturecontrolled crystallography if structural information on intermediate states were of interest.…”

Section: Temperature-controlled Kinetic Cryocrystallography To Characmentioning

confidence: 99%

Temperature-dependent macromolecular X-ray crystallography

Weik

Colletier

2010

Acta Crystallogr D Biol Cryst

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X-ray crystallography provides structural details of biological macromolecules. Whereas routine data are collected close to 100 K in order to mitigate radiation damage, more exotic temperature-controlled experiments in a broader temperature range from 15 K to room temperature can provide both dynamical and structural insights. Here, the dynamical behaviour of crystalline macromolecules and their surrounding solvent as a function of cryo-temperature is reviewed. Experimental strategies of kinetic crystallography are discussed that have allowed the generation and trapping of macromolecular intermediate states by combining reaction initiation in the crystalline state with appropriate temperature profiles. A particular focus is on recruiting X-ray-induced changes for reaction initiation, thus unveiling useful aspects of radiation damage, which otherwise has to be minimized in macromolecular crystallography.

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“…7 Similarly, recent crystallographic studies of cryotrapped CPO Compound III also were interpreted to lead to radiation-induced conversion to the hydroperoxo form, with no evidence for a trapped peroxo-ligated species. 25 Future studies with mutant proteins that NOT THE PUBLISHED VERSION; this is the author's final, peer-reviewed manuscript. The published version may be accessed by following the link in the citation at the bottom of the page.…”

mentioning

confidence: 99%

“…7 Similarly, recent crystallographic studies of cryotrapped CPO Compound III also were interpreted to lead to radiation-induced conversion to the hydroperoxo form, with no evidence for a trapped peroxo-ligated species. 25 Future studies with mutant proteins that Society and permission has been granted for this version to appear in e-Publications@Marquette. American Chemical Society does not grant permission for this article to be further copied/distributed or hosted elsewhere without the express permission from American Chemical Society.…”

mentioning

confidence: 99%

Resonance Raman Detection of the Hydroperoxo Intermediate in the Cytochrome P450 Enzymatic Cycle

et al. 2007

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The resonance Raman spectra of the hydroperoxo complex of camphor-bound CYP101 have been obtained by cryoradiolytic reduction of the oxygenated ferrous form that had been rapidly frozen in water/glycerol frozen solution; EPR spectroscopy was employed to confirm the identity of the trapped intermediate. The ν(O−O) mode, appearing at 799 cm -1 , is observed for the first time in a peroxo-heme adduct. It is assigned unambiguously by employing isotopomeric mixtures of oxygen gas containing 50% 16 O 18 O, confirming the presence of an intact O−O fragment. The ν(Fe−O) mode is observed at 559 cm -1 (H2O). Furthermore, both modes shift down by 3 cm -1 , documenting the formulation as a hydroperoxo complex, in agreement with EPR data.NOT THE PUBLISHED VERSION; this is the author's final, peer-reviewed manuscript. The published version may be accessed by following the link in the citation at the bottom of the page. Society, Vol 129, No. 20 (2007): pg. 6382-6383. DOI. This article is © American Chemical Society and permission has been granted for this version to appear in e-Publications@Marquette. American Chemical Society does not grant permission for this article to be further copied/distributed or hosted elsewhere without the express permission from American Chemical Society. Journal of the American Chemical 3The cytochromes P450 heme-thiolate enzymes facilitate quite difficult chemical transformations through a multistep reaction cycle that culminates in the generation of a remarkably potent oxidizing species capable of hydroxylating even inert substrates. [1][2][3] Following substrate binding to the resting state ferric enzyme, two sequential one-electron reductions bracketing the binding of molecular oxygen and a subsequent proton delivery step lead to heterolytic O−O bond cleavage and formation of a highly reactive ferryl heme species comparable to the so-called Compound I intermediate of peroxidases. [4][5][6] Thus, key precursors to this critical cleavage reaction are activated heme-bound peroxo and hydroperoxo fragments; that is, (protoporphyrin)Fe(III)(O2 2-) or Fe(III)(O−OH -). A useful approach to access and study these species is to generate and trap the relatively stable oxy-ferrous P450 complex and then to subject the cryotrapped (77 K) sample to radiolytic reduction using radiation from synchrotron, 60 Co γ-ray, or 32 P sources. 7,8 Enzymatic intermediates produced by cryoradiolytic reduction of the oxygenated complex of cytochrome P450cam (CYP101) have been detected by both electronic absorption and EPR spectroscopic methods. 7,9,10 However, critical mechanistic information has been missing, and it is now important to attempt to provide more detailed structural characterization of the active sites of these species.Resonance Raman (RR) spectroscopy is an especially attractive probe of such species, effectively interrogating both the heme macrocycle structure and various iron−ligand fragments. [11][12][13][14][15] In fact, the feasibility of coupling this powerful spectroscopic probe with cryogenic ...

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Structure and quantum chemical characterization of chloroperoxidase compound 0, a common reaction intermediate of diverse heme enzymes

Cited by 91 publications

References 56 publications

A peroxide bridge between Fe and Cu ions in the O ₂ reduction site of fully oxidized cytochrome c oxidase could suppress the proton pump

A peroxide bridge between Fe and Cu ions in the O ₂ reduction site of fully oxidized cytochrome c oxidase could suppress the proton pump

Temperature-dependent macromolecular X-ray crystallography

Resonance Raman Detection of the Hydroperoxo Intermediate in the Cytochrome P450 Enzymatic Cycle

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Structure and quantum chemical characterization of chloroperoxidase compound 0, a common reaction intermediate of diverse heme enzymes

Cited by 91 publications

References 56 publications

A peroxide bridge between Fe and Cu ions in the O 2 reduction site of fully oxidized cytochrome c oxidase could suppress the proton pump

A peroxide bridge between Fe and Cu ions in the O 2 reduction site of fully oxidized cytochrome c oxidase could suppress the proton pump

Temperature-dependent macromolecular X-ray crystallography

Resonance Raman Detection of the Hydroperoxo Intermediate in the Cytochrome P450 Enzymatic Cycle

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Product

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A peroxide bridge between Fe and Cu ions in the O ₂ reduction site of fully oxidized cytochrome c oxidase could suppress the proton pump

A peroxide bridge between Fe and Cu ions in the O ₂ reduction site of fully oxidized cytochrome c oxidase could suppress the proton pump