Role of Arginine Guanidinium Moiety in Nitric-oxide Synthase Mechanism of Oxygen Activation

Giroud, Claire; Moreau, Magali; Mattioli, Tony A.; Balland, Véronique; Boucher, Jean Luc; Xu-Li, Yun; Stuehr, Dennis J.; Santolini, Jérôme

doi:10.1074/jbc.m109.038240

Cited by 28 publications

(62 citation statements)

References 111 publications

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“…(55,71,72). Vibrational spectroscopies, such as resonance Raman and FTIR spectroscopies, allow the characterization of Fe-CO and C-O stretching modes.…”

Section: Trpmentioning

confidence: 99%

“…Data Analysis-Identification of spectral components in Raman and/or FTIR bands was achieved as previously described by the combination of Fourier self-deconvolution and second order derivative analysis of the averaged spectra using GRAMS 32 software (Galactic Industries, Salem, NH) (55). The overlapping peaks were resolved by fitting the spectral region to Lorentzian functions using Origin 6.0 (OriginLab Corp., Northampton, MA).…”

mentioning

confidence: 99%

“…The overlapping peaks were resolved by fitting the spectral region to Lorentzian functions using Origin 6.0 (OriginLab Corp., Northampton, MA). The NOS Raman bands were assigned following previous assignments on NOS (46,(55)(56)(57)(58)(59)(60). 66 bsNOS Mutants-The sulfur atom of NOS-proximal thiolate is naturally engaged in a strong H-bond interaction with the nitrogen proton of the indole ring of the vicinal tryptophan (see Scheme 1).…”

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confidence: 99%

“…the -competition between the distal and proximal ligands of the W66F/Y (respectively W66H) mutants (43,45,55).…”

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confidence: 99%

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The Proximal Hydrogen Bond Network Modulates Bacillus subtilis Nitric-oxide Synthase Electronic and Structural Properties

Brunel

Wilson

Henry

et al. 2011

Journal of Biological Chemistry

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Bacterial nitric-oxide synthase (NOS)-like proteins are believed to be genuine NOSs. As for cytochromes P450 (CYPs), NOS-proximal ligand is a thiolate that exerts a push effect crucial for the process of dioxygen activation. Unlike CYPs, this catalytic electron donation seems controlled by a hydrogen bond (H-bond) interaction between the thiolate ligand and a vicinal tryptophan. Variations of the strength of this H-bond could provide a direct way to tune the stability along with the electronic and structural properties of NOS. We generated five different mutations of bsNOS Trp 66 , which can modulate this proximal H-bond. We investigated the effects of these mutations on different NOS complexes (Fe III , Fe II CO, and Fe II NO), using a combination of UV-visible absorption, EPR, FTIR, and resonance Raman spectroscopies. Our results indicate that (i) the proximal H-bond modulation can selectively decrease or increase the electron donating properties of the proximal thiolate, (ii) this modulation controls the -competition between distal and proximal ligands, (iii) this H-bond controls the stability of various NOS intermediates, and (iv) a fine tuning of the electron donation by the proximal ligand is required to allow at the same time oxygen activation and to prevent uncoupling reactions.

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“…(55,71,72). Vibrational spectroscopies, such as resonance Raman and FTIR spectroscopies, allow the characterization of Fe-CO and C-O stretching modes.…”

Section: Trpmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

“…the -competition between the distal and proximal ligands of the W66F/Y (respectively W66H) mutants (43,45,55).…”

mentioning

confidence: 99%

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The Proximal Hydrogen Bond Network Modulates Bacillus subtilis Nitric-oxide Synthase Electronic and Structural Properties

Brunel

Wilson

Henry

et al. 2011

Journal of Biological Chemistry

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“…2 In the second step of the reaction, another molecule of O 2 and an additional electron from NADPH are used to convert NOHA to L-citrulline and NO. Previous studies suggest that the two steps of the reaction follow distinct mechanisms meditated by a compound I (Cmpd I) type of ferryl intermediate and a peroxyl intermediate, respectively (1)(2)(3)(4)(5)(6)(7). These mechanisms, however, remain elusive, as none of the putative intermediates have been experimentally observed under solution conditions, although (hydro)peroxo intermediates have been identified at cryogenic temperatures by radiolytic reduction methods (8,9); in addition, a Cmpd I intermediate has been observed after peroxyacid treatment (10).…”

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confidence: 99%

Catalytic Intermediates of Inducible Nitric-oxide Synthase Stabilized by the W188H Mutation*

Sabat

Egawa

et al. 2013

Journal of Biological Chemistry

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Oxygen activation in NO synthases: evidence for a direct role of the substrate

et al. 2016

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Nitric oxide ( NO ) and the other reactive nitrogen species ( RNOS ) play crucial patho‐physiological roles at the interface of oxidative stress and signalling processes. In mammals, the NO synthases ( NOS s) are the source of these reactive nitrogen species, and so to understand the precise biological role of RNOS and NO requires elucidation of the molecular functioning of NOS . Oxygen activation, which is at the core of NOS catalysis, involves a sophisticated sequence of electron and proton transfers. While electron transfer in NOS has received much attention, the proton transfer processes has been scarcely investigated. Here, we report an original approach that combines fast‐kinetic techniques coupled to resonance Raman spectroscopy with the use of synthetic analogues of NOS substrate. We characterise Fe II ‐O 2 reaction intermediates in the presence of L‐arginine (Arg), alkyl‐ and aryl‐guanidines. The presence of new reaction intermediates, such as ferric haem‐peroxide, that was formerly postulated, was tracked by analysing the oxygen activation reaction at different times and with different excitation wavelengths. Our results suggest that Arg is not a proton donor, but indirectly intervenes in oxygen activation mechanism by modulating the distal H‐bond network and, in particular, by tuning the position and the role of the distal water molecule. This report supports a catalytic model with two proton transfers in step 1 (Arg hydroxylation) but only one proton transfer in step 2 (N ω ‐hydroxy‐L‐arginine oxidation).

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Role of Arginine Guanidinium Moiety in Nitric-oxide Synthase Mechanism of Oxygen Activation

Cited by 28 publications

References 111 publications

The Proximal Hydrogen Bond Network Modulates Bacillus subtilis Nitric-oxide Synthase Electronic and Structural Properties

The Proximal Hydrogen Bond Network Modulates Bacillus subtilis Nitric-oxide Synthase Electronic and Structural Properties

Catalytic Intermediates of Inducible Nitric-oxide Synthase Stabilized by the W188H Mutation*

Oxygen activation in NO synthases: evidence for a direct role of the substrate

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