Sulfide binding properties of truncated hemoglobins
The truncated hemoglobins from Bacillus subtilis (Bs-trHb) and Thermobifida fusca (Tf-trHb) have been shown to form high-affinity complexes with hydrogen sulfide in their ferric state. The recombinant proteins, as extracted, from Escherichia coli cells after overexpression, are indeed partially satu...
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2010
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| LEADER | 16721caa a22018617a 4500 | ||
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| 001 | PAPER-22934 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518205433.0 | ||
| 008 | 190411s2010 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-77949408968 | |
| 024 | 7 | |2 cas |a cysteine, 4371-52-2, 52-89-1, 52-90-4; ferric ion, 20074-52-6; hydrogen sulfide, 15035-72-0, 7783-06-4; Bacterial Proteins; Sulfides; Truncated Hemoglobins | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a BICHA | ||
| 100 | 1 | |a Nicoletti, F.P. | |
| 245 | 1 | 0 | |a Sulfide binding properties of truncated hemoglobins |
| 260 | |c 2010 | ||
| 270 | 1 | 0 | |m Boffi, A.; Istituto Pasteur, Fondazione Cenci-Bolognetti, Department of Biochemical Sciences, University of Rome la Sapienza, Piazzale Aldo Moro 5, 1-00185 Rome, Italy; email: alberto.boffi@uniromal.it |
| 506 | |2 openaire |e Política editorial | ||
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| 520 | 3 | |a The truncated hemoglobins from Bacillus subtilis (Bs-trHb) and Thermobifida fusca (Tf-trHb) have been shown to form high-affinity complexes with hydrogen sulfide in their ferric state. The recombinant proteins, as extracted, from Escherichia coli cells after overexpression, are indeed partially saturated with sulfide, and even highly purified samples still contain a small but significant amount of iron-bound sulfide. Thus, a complete thermodynamic and kinetic study has been undertaken by means of equilibrium and kinetic displacement experiments to assess the relevant sulfide binding parameters. The body of experimental data indicates that both proteins possess a high, affinity for hydrogen sulfide (K= 5.0 × 106 and 28 × 106 M-1 for Bs-trHb and Tf-trHb, respectively, at pH 7.0), though, lower with, respect to that reported previously for the sulfide avid Lucina pectinata I hemoglobins (2.9 × 108 M-1). From the kinetic point of view, the overall high affinity resides in the slow rate of sulfide release, attributed to hydrogen bonding stabilization of the bound ligand by distal residue WG8. A set of point mutants in which these residues have been replaced with Phe indicates that the WG8 residue represents the major kinetic barrier to the escape of the bound sulfide species. Accordingly, classical molecular dynamics simulations of SH.....-bound ferric Tf-trHb show that WG8 plays a key role in the stabilization of coordinated SH -whereas the YCD1 and. YB10 contributions are negligible. Interestingly, the triple Tf-trHb mutant bearing only Phe residues in the relevant B10, G8, and CD1 positions is endowed with a higher overall affinity for sulfide characterized, by a very fast second-order rate constant and 2 order of magnitude faster kinetics of sulfide release with respect to the wild-type protein. Resonance Raman spectroscopy data indicate that the sulfide adducts are typical of a ferric iron, low-spin derivative. In analogy with other low-spin ferric sulfide adducts, the strong band at 375 cm-1 is tentatively assigned to a Fe-S stretching band. The high affinity for hydrogen, sulfide is thought to have a possible physiological significance as H2S is produced in bacteria at metabolic steps involved in cysteine biosynthesis and hence in thiol redox homeostasis. © 2010 American Chemical Society. |l eng | |
| 593 | |a Istituto Pasteur, Fondazione Cenci-Bolognetti, Department of Biochemical Sciences, University of Rome la Sapienza, Piazzale Aldo Moro 5, 1-00185 Rome, Italy | ||
| 593 | |a Dipartimento di Chimica, Università di Firenze, Via della Lastruccia 3, I-50019 Sesto Fiorentino (FI), Italy | ||
| 593 | |a Departamento de Química Inorgánica, Analítica, y Química Física, INQUIMAE-CONICET, Ciudad Universitaria, Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a BACILLUS SUBTILIS |
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| 690 | 1 | 0 | |a BINDING PARAMETER |
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| 690 | 1 | 0 | |a CLASSICAL MOLECULAR DYNAMICS |
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| 690 | 1 | 0 | |a SECOND-ORDER RATE CONSTANTS |
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| 690 | 1 | 0 | |a RATE CONSTANTS |
| 690 | 1 | 0 | |a SPIN DYNAMICS |
| 690 | 1 | 0 | |a STABILIZATION |
| 690 | 1 | 0 | |a SULFUR DETERMINATION |
| 690 | 1 | 0 | |a HYDROGEN SULFIDE |
| 690 | 1 | 0 | |a BACTERIAL PROTEIN |
| 690 | 1 | 0 | |a CYSTEINE |
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| 700 | 1 | |a Bonamore, A. | |
| 700 | 1 | |a Boechi, L. | |
| 700 | 1 | |a Boubeta, F.M. | |
| 700 | 1 | |a Feis, A. | |
| 700 | 1 | |a Smulevich, I. | |
| 700 | 1 | |a Boffi, A. | |
| 773 | 0 | |d 2010 |g v. 49 |h pp. 2269-2278 |k n. 10 |p Biochemistry |x 00062960 |w (AR-BaUEN)CENRE-755 |t Biochemistry | |
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