Heme pocket structural properties of a bacterial truncated hemoglobin from thermobifida fusca
An acidic surface variant (ASV) of the "truncated" hemoglobin from Thermobifida fusca was designed with the aim of creating a versatile globin scaffold endowed with thermostability and a high level of recombinant expression in its soluble form while keeping the active site unmodified. This...
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| Otros Autores: | , , , , , , , |
| Formato: | Capítulo de libro |
| Lenguaje: | Inglés |
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2010
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| LEADER | 16874caa a22015977a 4500 | ||
|---|---|---|---|
| 001 | PAPER-22768 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518205421.0 | ||
| 008 | 190411s2010 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-78650113583 | |
| 024 | 7 | |2 cas |a arginine, 1119-34-2, 15595-35-4, 7004-12-8, 74-79-3; carbon monoxide, 630-08-0; glutamic acid, 11070-68-1, 138-15-8, 56-86-0, 6899-05-4; heme, 14875-96-8; histidine, 645-35-2, 7006-35-1, 71-00-1; iron, 14093-02-8, 53858-86-9, 7439-89-6; phenylalanine, 3617-44-5, 63-91-2; tyrosine, 16870-43-2, 55520-40-6, 60-18-4; Bacterial Proteins; Heme, 14875-96-8; Recombinant Proteins; Truncated Hemoglobins | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a BICHA | ||
| 100 | 1 | |a Droghetti, E. | |
| 245 | 1 | 0 | |a Heme pocket structural properties of a bacterial truncated hemoglobin from thermobifida fusca |
| 260 | |c 2010 | ||
| 270 | 1 | 0 | |m Feis, A.; Dipartimento di Chimica Ugo Schiff, Università di Firenze, Via della Lastruccia 3, I-50019 Sesto Fiorentino (FI), Italy; email: alessandro.feis@unifi.it |
| 506 | |2 openaire |e Política editorial | ||
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| 520 | 3 | |a An acidic surface variant (ASV) of the "truncated" hemoglobin from Thermobifida fusca was designed with the aim of creating a versatile globin scaffold endowed with thermostability and a high level of recombinant expression in its soluble form while keeping the active site unmodified. This engineered protein was obtained by mutating the surface-exposed residues Phe107 and Arg91 to Glu. Molecular dynamics simulations showed that the mutated residues remain solvent-exposed, not affecting the overall protein structure. Thus, the ASV was used in a combinatorial mutagenesis of the distal heme pocket residues in which one, two, or three of the conserved polar residues [TyrB10(54), TyrCD1(67), and TrpG8(119)] were substituted with Phe. Mutants were characterized by infrared and resonance Raman spectroscopy and compared with the wild-type protein. Similar Fe-proximal His stretching frequencies suggest that none of the mutations alters the proximal side of the heme cavity. Two conformers were observed in the spectra of the CO complexes of both wild-type and ASV protein: form 1 with v(FeC) and v(CO) at 509 and 1938 cm-1 and form 2 with v(FeC) and v(CO) at 518 and 1920 cm-1, respectively. Molecular dynamics simulations were performed for the wild-type and ASV forms, as well as for the TyrB10 mutant. The spectroscopic and computational results demonstrate that CO interacts with TrpG8 in form 1 and interacts with both TrpG8 and TyrCD1 in form 2. TyrB10 does not directly interact with the bound CO. © 2010 American Chemical Society. |l eng | |
| 593 | |a Dipartimento di Chimica Ugo Schiff, Università di Firenze, Via della Lastruccia 3, I-50019 Sesto Fiorentino (FI), Italy | ||
| 593 | |a Department of Biochemical Sciences, CNR Institute of Molecular Biology and Pathology, University of Rome La Sapienza, Piazzale Aldo Moro 5, I-00185 Rome, Italy | ||
| 593 | |a Departamento de Química Inorgánica, Analítica y Química Física/INQUIMAE-CONICET, Universidad de Buenos Aires, Pabellón II (C1428EHA), Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a ACIDIC SURFACE |
| 690 | 1 | 0 | |a ACTIVE SITE |
| 690 | 1 | 0 | |a CO COMPLEXES |
| 690 | 1 | 0 | |a COMPUTATIONAL RESULTS |
| 690 | 1 | 0 | |a CONSERVED POLAR RESIDUES |
| 690 | 1 | 0 | |a HEME POCKETS |
| 690 | 1 | 0 | |a MOLECULAR DYNAMICS SIMULATIONS |
| 690 | 1 | 0 | |a PROTEIN STRUCTURES |
| 690 | 1 | 0 | |a RECOMBINANT EXPRESSION |
| 690 | 1 | 0 | |a RESONANCE RAMAN SPECTROSCOPY |
| 690 | 1 | 0 | |a STRETCHING FREQUENCY |
| 690 | 1 | 0 | |a THERMOBIFIDA FUSCA |
| 690 | 1 | 0 | |a TRUNCATED HEMOGLOBINS |
| 690 | 1 | 0 | |a WILD TYPES |
| 690 | 1 | 0 | |a WILD-TYPE PROTEINS |
| 690 | 1 | 0 | |a HEMOGLOBIN |
| 690 | 1 | 0 | |a PORPHYRINS |
| 690 | 1 | 0 | |a RAMAN SPECTROSCOPY |
| 690 | 1 | 0 | |a MOLECULAR DYNAMICS |
| 690 | 1 | 0 | |a ARGININE |
| 690 | 1 | 0 | |a CARBON MONOXIDE |
| 690 | 1 | 0 | |a GLUTAMIC ACID |
| 690 | 1 | 0 | |a HEME |
| 690 | 1 | 0 | |a HISTIDINE |
| 690 | 1 | 0 | |a IRON |
| 690 | 1 | 0 | |a PHENYLALANINE |
| 690 | 1 | 0 | |a TRUNCATED HEMOGLOBIN |
| 690 | 1 | 0 | |a TYROSINE |
| 690 | 1 | 0 | |a ACIDIC SURFACE VARIANT |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a BACTERIUM |
| 690 | 1 | 0 | |a HYDROGEN BOND |
| 690 | 1 | 0 | |a INFRARED SPECTROSCOPY |
| 690 | 1 | 0 | |a MOLECULAR DYNAMICS |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a PROTEIN STRUCTURE |
| 690 | 1 | 0 | |a RAMAN SPECTROMETRY |
| 690 | 1 | 0 | |a SIMULATION |
| 690 | 1 | 0 | |a THERMOBIFIDA FUSCA |
| 690 | 1 | 0 | |a THERMOSTABILITY |
| 690 | 1 | 0 | |a ACTINOMYCETALES |
| 690 | 1 | 0 | |a BACTERIAL PROTEINS |
| 690 | 1 | 0 | |a HEME |
| 690 | 1 | 0 | |a MUTATION |
| 690 | 1 | 0 | |a PROTEIN BINDING |
| 690 | 1 | 0 | |a RECOMBINANT PROTEINS |
| 690 | 1 | 0 | |a TRUNCATED HEMOGLOBINS |
| 690 | 1 | 0 | |a BACTERIA (MICROORGANISMS) |
| 690 | 1 | 0 | |a THERMOBIFIDA FUSCA |
| 650 | 1 | 7 | |2 spines |a MUTAGENESIS |
| 700 | 1 | |a Nicoletti, F.P. | |
| 700 | 1 | |a Bonamore, A. | |
| 700 | 1 | |a Boechi, L. | |
| 700 | 1 | |a Arroyo Mañez, P. | |
| 700 | 1 | |a Estrin, D.A. | |
| 700 | 1 | |a Boffi, A. | |
| 700 | 1 | |a Smulevich, G. | |
| 700 | 1 | |a Feis, A. | |
| 773 | 0 | |d 2010 |g v. 49 |h pp. 10394-10402 |k n. 49 |p Biochemistry |x 00062960 |w (AR-BaUEN)CENRE-755 |t Biochemistry | |
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