title: Motion of proximal histidine and structural allosteric transition in soluble guanylate cyclase.
abstract: We investigated the changes of heme coordination in purified soluble guanylate cyclase (sGC) by time-resolved spectroscopy in a time range encompassing 11 orders of magnitude (from 1 ps to 0.2 s). After dissociation, NO either recombines geminately to the 4-coordinate (4c) heme (τG1 = 7.5 ps; 97 ± 1% of the population) or exits the heme pocket (3 ± 1%). The proximal His rebinds to the 4c heme with a 70-ps time constant. Then, NO is distributed in two approximately equal populations (1.5%). One geminately rebinds to the 5c heme (τG2 = 6.5 ns), whereas the other diffuses out to the solution, from where it rebinds bimolecularly (τ = 50 μs with [NO] = 200 μM) forming a 6c heme with a diffusion-limited rate constant of 2 × 10(8) M(-1)⋅s(-1). In both cases, the rebinding of NO induces the cleavage of the Fe-His bond that can be observed as an individual reaction step. Saliently, the time constant of bond cleavage differs depending on whether NO binds geminately or from solution (τ5C1 = 0.66 μs and τ5C2 = 10 ms, respectively). Because the same event occurs with rates separated by four orders of magnitude, this measurement implies that sGC is in different structural states in both cases, having different strain exerted on the Fe-His bond. We show here that this structural allosteric transition takes place in the range 1-50 μs. In this context, the detection of NO binding to the proximal side of sGC heme is discussed.
authors.affiliation: Laboratoire d'Optique et Biosciences, INSERM U1182, Ecole Polytechnique, 91128 Palaiseau Cedex, France; and.
authors.forename: Byung-Kuk
authors.initials: BK
authors.lastname: Yoo
authors.affiliation: Laboratoire d'Optique et Biosciences, INSERM U1182, Ecole Polytechnique, 91128 Palaiseau Cedex, France; and.
authors.forename: Isabelle
authors.initials: I
authors.lastname: Lamarre
authors.affiliation: Laboratoire d'Optique et Biosciences, INSERM U1182, Ecole Polytechnique, 91128 Palaiseau Cedex, France; and.
authors.forename: Jean-Louis
authors.initials: JL
authors.lastname: Martin
authors.affiliation: Laboratoire de Physiologie Membranaire et Moléculaire du Chloroplaste, UMR7141, Institut de Biologie Physico-Chimie, 75005 Paris, France.
authors.forename: Fabrice
authors.initials: F
authors.lastname: Rappaport
authors.affiliation: Laboratoire d'Optique et Biosciences, INSERM U1182, Ecole Polytechnique, 91128 Palaiseau Cedex, France; and michel.negrerie@polytechnique.fr.
authors.forename: Michel
authors.initials: M
authors.lastname: Negrerie
mesh_terms: D000495:Allosteric Site; D000818:Animals; D002417:Cattle; D006162:Guanylate Cyclase / Q000737:chemistry*; D006418:Heme / Q000737:chemistry; D006454:Hemoglobins / Q000737:chemistry; D006639:Histidine / Q000737:chemistry*; D007501:Iron / Q000737:chemistry; D008968:Molecular Conformation; D009569:Nitric Oxide / Q000737:chemistry; D011485:Protein Binding; D018160:Receptors, Cytoplasmic and Nuclear / Q000737:chemistry*; D015398:Signal Transduction; D000071756:Soluble Guanylyl Cyclase; D013053:Spectrophotometry; D013997:Time Factors
chemical_list: D006454:Hemoglobins; D018160:Receptors, Cytoplasmic and Nuclear; D009569:Nitric Oxide; D006418:Heme; D006639:Histidine; D007501:Iron; D006162:Guanylate Cyclase; D000071756:Soluble Guanylyl Cyclase
keywords: allostery; nitric oxide; protein activation; soluble guanylate cyclase; time-resolved absorption spectroscopy
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