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Howes, B.D.; Giordano, D.; Boechi, L.; Russo, R.; Mucciacciaro, S.; Ciaccio, C.; Sinibaldi, F.; Fittipaldi, M.; Martí, M.A.; Estrin, D.A.; Di Prisco, G.; Coletta, M.; Verde, C.; Smulevich, G. "The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125" (2011) Journal of Biological Inorganic Chemistry. 16(2):299-311
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Abstract:

The genome of the cold-adapted bacterium Pseudoalteromonas haloplanktis TAC125 contains multiple genes encoding three distinct monomeric hemoglobins exhibiting a 2/2 α-helical fold. In the present work, one of these hemoglobins is studied by resonance Raman, electronic absorption and electronic paramagnetic resonance spectroscopies, kinetic measurements, and different bioinformatic approaches. It is the first cold-adapted bacterial hemoglobin to be characterized. The results indicate that this protein belongs to the 2/2 hemoglobin family, Group II, characterized by the presence of a tryptophanyl residue on the bottom of the heme distal pocket in position G8 and two tyrosyl residues (TyrCD1 and TyrB10). However, unlike other bacterial hemoglobins, the ferric state, in addition to the aquo hexacoordinated high-spin form, shows multiple hexacoordinated low-spin forms, where either TyrCD1 or TyrB10 can likely coordinate the iron. This is the first example in which both TyrCD1 and TyrB10 are proposed to be the residues that are alternatively involved in heme hexacoordination by endogenous ligands. © 2010 SBIC.

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Documento: Artículo
Título:The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125
Autor:Howes, B.D.; Giordano, D.; Boechi, L.; Russo, R.; Mucciacciaro, S.; Ciaccio, C.; Sinibaldi, F.; Fittipaldi, M.; Martí, M.A.; Estrin, D.A.; Di Prisco, G.; Coletta, M.; Verde, C.; Smulevich, G.
Filiación:Dipartimento di Chimica, Università di Firenze, Sesto Fiorentino (FI) 50019, Italy
INSTM (Consorzio Interuniversitario per la Scienza e Tecnologia Dei Materiali), Sesto Fiorentino (FI) 50019, Italy
Institute of Protein Biochemistry, CNR, Naples 80131, Italy
Departemento de Química Inorgánica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires C1428EHA, Argentina
Dipartimento di Medicina Sperimentale e Scienze Biochimiche, Università di Roma Tor Vergata, Rome 00133, Italy
Consorzio Interuniversitario di Ricerca in Chimica Dei Metalli Nei Sistemi Biologici, Bari 70126, Italy
Palabras clave:Antarctic bacterium; EPR; Molecular dynamics; Resonance Raman; Tyrosinate ligand; bacterial protein; hemoglobin; protein TAC125; tryptophan; tyrosine; unclassified drug; article; Bacillus subtilis; cold acclimatization; controlled study; crystal structure; gene overexpression; gene sequence; Geobacillus stearothermophilus; molecular cloning; molecular dynamics; Mycobacterium tuberculosis; nonhuman; oxidation reduction potential; priority journal; protein analysis; protein purification; protein structure; Pseudoalteromonas; Pseudoalteromonas haloplanktis; Raman spectrometry; sequence alignment; Shewanella oneidensis; simulation; Bacterial Proteins; Electrochemistry; Electron Spin Resonance Spectroscopy; Hemoglobins; Molecular Dynamics Simulation; Oxidation-Reduction; Pseudoalteromonas; Temperature; Bacteria (microorganisms); Pseudoalteromonas haloplanktis
Año:2011
Volumen:16
Número:2
Página de inicio:299
Página de fin:311
DOI: http://dx.doi.org/10.1007/s00775-010-0726-y
Título revista:Journal of Biological Inorganic Chemistry
Título revista abreviado:J. Biol. Inorg. Chem.
ISSN:09498257
CODEN:JJBCF
CAS:hemoglobin, 9008-02-0; tryptophan, 6912-86-3, 73-22-3; tyrosine, 16870-43-2, 55520-40-6, 60-18-4; Bacterial Proteins; Hemoglobins
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09498257_v16_n2_p299_Howes

Referencias:

  • Deming, J.W., Psychrophiles and polar regions (2002) Current Opinion in Microbiology, 5 (3), pp. 301-309. , DOI 10.1016/S1369-5274(02)00329-6
  • Medigue, C., Krin, E., Pascal, G., Barbe, V., Bernsel, A., Bertin, P.N., Cheung, F., Danchin, A., Coping with cold: The genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125 (2005) Genome Research, 15 (10), pp. 1325-1335. , http://www.genome.org/cgi/reprint/15/10/1325, DOI 10.1101/gr.4126905
  • Giordano, D., Parrilli, E., Dettai, A., Russo, R., Barbiero, G., Marino, G., Lecointre, G., Verde, C., The truncated hemoglobins in the Antarctic psychrophilic bacterium Pseudoalteromonas haloplanktis TAC125 (2007) Gene, 398 (1-2 SPEC. ISS.), pp. 69-77. , DOI 10.1016/j.gene.2007.02.037, PII S0378111907002156
  • Nicoletti, F.P., Comandini, A., Bonamore, A., Boechi, L., Boubeta, F., Feis, A., Smulevich, G., Boffi, A., (2010) Biochemistry, 49, pp. 2269-2278. , 1:CAS:528:DC%2BC3cXitFaqur4%3D 10.1021/bi901671d 20102180
  • Kraus, D.W., Wittenberg, J.B., Lu, J.F., Peisach, J., (1990) J Biol Chem, 265, pp. 16054-16059. , 1:CAS:528:DyaK3MXhtlyhs7w%3D 2168877
  • Brittain, T., Yosaatmadja, Y., Henty, K., (2008) IUBMB Life, 60, pp. 135-138. , 1:CAS:528:DC%2BD1cXhtlKnu7rI 10.1002/iub.16 18380003
  • Ferri, T., Poscia, A., Santucci, R., Direct electrochemistry of membrane-entrapped horseradish peroxidase. Part I. A voltammetric and spectroscopic study (1998) Bioelectrochemistry and Bioenergetics, 44 (2), pp. 177-181. , DOI 10.1016/S0302-4598(97)00088-3, PII S0302459897000883
  • Nicoletti, F.P., Thompson, M., Howes, B.D., Franzen, S., Smulevich, G., (2010) Biochemistry, 49, pp. 1903-1912. , 1:CAS:528:DC%2BC3cXhslSgtL0%3D 10.1021/bi9020567 20073507
  • Sali, A., Blundell, T.L., Comparative protein modelling by satisfaction of spatial restraints (1993) Journal of Molecular Biology, 234 (3), pp. 779-815. , DOI 10.1006/jmbi.1993.1626
  • Tatusova, T.A., Madden, T.L., (1999) FEMS Microbiol Lett, 174, pp. 247-250. , 1:CAS:528:DyaK1MXjtlOlu74%3D 10.1111/j.1574-6968.1999.tb13575.x 10339815
  • Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F., Higgins, D.G., The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools (1997) Nucleic Acids Research, 25 (24), pp. 4876-4882. , DOI 10.1093/nar/25.24.4876
  • Pearlman, D.A., Case, D.A., Caldwell, J.W., Ross, W.S., Cheatham, T.E., Debolt, S., Ferguson, D., Kollman, P., (1995) Comput Phys Commun, 91, pp. 1-41. , 1:CAS:528:DyaK2MXps1Wrtrw%3D 10.1016/0010-4655(95)00041-D
  • Boechi, L., Martí, M.A., Milani, M., Bolognesi, M., Luque, F.J., Estrin, D.A., (2008) Proteins, 73, pp. 372-379. , 1:CAS:528:DC%2BD1cXhtFOisb3J 10.1002/prot.22072 18433052
  • Boechi, L., Manez, P.A., Luque, F.J., Marti, M.A., Estrin, D.A., (2010) Proteins, 78, pp. 962-970. , 1:CAS:528:DC%2BC3cXhtVSlsbw%3D 10.1002/prot.22620 19899166
  • Marti, M.A., Capece, L., Bidon-Chanal, A., Crespo, A., Guallar, V., Luque, F.J., Estrin, D.A., (2008) Methods Enzymol, 437, pp. 477-498. , 1:CAS:528:DC%2BD1cXntF2ht7g%3D 10.1016/S0076-6879(07)37024-9 18433643
  • Milani, M., Pesce, A., Nardini, M., Ouellet, H., Ouellet, Y., Dewilde, S., Bocedi, A., Bolognesi, M., Structural bases for heme binding and diatomic ligand recognition in truncated hemoglobins (2005) Journal of Inorganic Biochemistry, 99 (1), pp. 97-109. , DOI 10.1016/j.jinorgbio.2004.10.035, PII S0162013404003423, Heme-Diatomic Interactions, Part 1
  • Wittenberg, J.B., Bolognesi, M., Wittenberg, B.A., Guertin, M., Truncated hemoglobins: A new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants (2002) Journal of Biological Chemistry, 277 (2), pp. 871-874. , DOI 10.1074/jbc.R100058200
  • Vuletich, D.A., Lecomte, J.T., (2006) J Mol Evol, 62, pp. 196-210. , 1:CAS:528:DC%2BD28XitV2qurg%3D 10.1007/s00239-005-0077-4 16474979
  • Antonini, E., Brunori, M., (1971) Hemoglobin and Myoglobin in Their Reactions with Ligands, , North-Holland Amsterdam
  • Das, T.K., Couture, M., Lee, H.C., Peisach, J., Rousseau, D.L., Wittenberg, B.A., Wittenberg, J.B., Guertin, M., (1999) Biochemistry, 38, pp. 15360-15368. , 1:CAS:528:DyaK1MXmslCltbs%3D 10.1021/bi991237e 10563822
  • Caillet-Saguy, C., Turano, P., Piccioli, M., Lukat-Rodgers, G.S., Czjzek, M., Guigliarelli, B., Izadi-Pruneyre, N., Lecroisey, A., (2008) J Biol Chem, 283, pp. 5960-5970. , 1:CAS:528:DC%2BD1cXit1Omu78%3D 10.1074/jbc.M703795200 18162469
  • Alontaga, A.Y., Rodriguez, J.C., Schonbrunn, E., Becker, A., Funke, T., Yukl, E.T., Hayashi, T., Rivera, M., (2009) Biochemistry, 48, pp. 96-109. , 1:CAS:528:DC%2BD1cXhsVyksrbP 10.1021/bi801860g 19072037
  • Smulevich, G., Miller, M.A., Kraut, J., Spiro, T.G., (1991) Biochemistry, 30, pp. 9546-9558. , 1:CAS:528:DyaK3MXlsFersbs%3D 10.1021/bi00103a023 1654102
  • Smulevich, G., Wang, Y., Edwards, S.L., Poulos, T.L., English, A.M., Spiro, T.G., (1990) Biochemistry, 29, pp. 2586-2592. , 1:CAS:528:DyaK3cXhtFCku7c%3D 10.1021/bi00462a022 2159325
  • Smulevich, G., Paoli, M., Burke, J.F., Sanders, S.A., Thorneley, R.N.F., Smith, A.T., Characterization of recombinant horseradish peroxidase C and three site- directed mutants, F41V, F41W, and R38K, by resonance Raman spectroscopy (1994) Biochemistry, 33 (23), pp. 7398-7407. , DOI 10.1021/bi00189a046
  • Smulevich, G., Feis, A., Focardi, C., Tams, J., Welinder, K.G., (1994) Biochemistry, 33, pp. 15425-15432. , 1:CAS:528:DyaK2MXit1Smsrc%3D 10.1021/bi00255a024 7803406
  • Que, L., Metal-tyrosinate proteins (1988) Biological Applications of Raman Spectroscopy, 3, pp. 491-521. , T.G. Spiro (eds). Wiley New York
  • Hu, S., Smith, K.M., Spiro, T.G., Assignment of protoheme Resonance Raman spectrum by heme labeling in myoglobin (1996) Journal of the American Chemical Society, 118 (50), pp. 12638-12646. , DOI 10.1021/ja962239e, PII S0002786396022391
  • Nagai, K., Kagimoto, T., Hayashi, A., Taketa, F., Kitagawa, T., (1983) Biochemistry, 22, pp. 1305-1311. , 1:CAS:528:DyaL3sXhtVaqsbY%3D 10.1021/bi00274a048 6838855
  • Nagai, M., Yoneyama, Y., Kitagawa, T., Characteristics in tyrosine coordinations of four hemoglobins M probed by resonance Raman spectroscopy (1989) Biochemistry, 28 (6), pp. 2418-2422. , DOI 10.1021/bi00432a012
  • Adachi, S.-I., Nagano, S., Ishimori, K., Watanabe, Y., Morishima, I., Egawa, T., Kitagawa, T., Makino, R., Roles of proximal ligand in heme proteins: Replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase (1993) Biochemistry, 32 (1), pp. 241-252. , DOI 10.1021/bi00052a031
  • Liu, Y., Moenne-Loccoz, P., Hildebrand, D.P., Wilks, A., Loehr, T.M., Mauk, A.G., Ortiz De Montellano, P.R., Replacement of the proximal histidine iron ligand by a cysteine or tyrosine converts heme oxygenase to an oxidase (1999) Biochemistry, 38 (12), pp. 3733-3743. , DOI 10.1021/bi982707s
  • Eakanunkul, S., Lukat-Rodgers, G.S., Sumithran, S., Ghosh, A., Rodgers, K.R., Dawson, J.H., Wilks, A., Characterization of the periplasmic heme-binding protein ShuT from the heme uptake system of Shigella dysenteriae (2005) Biochemistry, 44 (39), pp. 13179-13191. , DOI 10.1021/bi050422r
  • Aki, Y., Nagai, M., Nagai, Y., Imai, K., Aki, M., Sato, A., Kubo, M., Kitagawa, T., (2010) J Biol Inorg Chem, 15, pp. 147-158. , 1:CAS:528:DC%2BD1MXhtVaqt7zO 10.1007/s00775-009-0579-4 19701784
  • Howes, B.D., Feis, A., Indiani, C., Marzocchi, M.P., Smulevich, G., (2000) J Biol Inorg Chem, 5, pp. 227-235. , 1:CAS:528:DC%2BD3cXjtVejtLs%3D 10.1007/s007750050367 10819468
  • Blumberg, W.E., Peisach, J., Probes of structure and function of macromolecules and membranes (1971) Probes of Enzymes and Hemoproteins, pp. 215-228. , Chance B, Yonetani T, Mildvan AS (eds) Academic, New York
  • Brautigan, D.L., Feinberg, B.A., Hoffman, B.M., Margoliash, E., Peisach, J., Blumberg, W.E., (1977) J Biol Chem, 252, pp. 574-582. , 1:CAS:528:DyaE2sXosFSnsA%3D%3D 13072
  • Walker, F.A., Huynh, B.H., Scheidt, W.R., Osvath, S.R., (1986) J Am Chem Soc, 108, pp. 5288-5297. , 1:CAS:528:DyaL28XkslCmtr8%3D 10.1021/ja00277a038
  • Izadi, N., Henry, Y., Haladjian, J., Goldberg, M.E., Wandersman, C., Delepierre, M., Lecroisey, A., Purification and characterization of an extracellular heme-binding protein, HasA, involved in heme iron acquisition (1997) Biochemistry, 36 (23), pp. 7050-7057. , DOI 10.1021/bi962577s
  • Arnoux, P., Haser, R., Izadi, N., Lecroisey, A., Delepierre, M., Wandersman, C., Czjzek, M., The crystal structure of HasA, a hemophore secreted by Serratia marcescens (1999) Nature Structural Biology, 6 (6), pp. 516-520. , DOI 10.1038/9281
  • Nicoletti, F.P., Howes, B.D., Fittipaldi, M., Fanali, G., Fasano, M., Ascenzi, P., Smulevich, G., (2008) J Am Chem Soc, 130, pp. 11677-11688. , 1:CAS:528:DC%2BD1cXptl2gtrg%3D 10.1021/ja800966t 18681435
  • Teixeira, M., Campos, A.P., Aguiar, A.P., Costa, H.S., Santos, H., Turner, D.L., Xavier, A.V., Pitfalls in assigning heme axial coordination by EPR. c-Type cytochromes with atypical Met-His ligation (1993) FEBS Letters, 317 (3), pp. 233-236. , DOI 10.1016/0014-5793(93)81282-5
  • Palmer, G., (1985) Biochem Soc Trans, 13, pp. 548-560. , 1:CAS:528:DyaL2MXltVWjsb0%3D 2993061
  • Taylor, C.P.S., (1977) Biochim Biophys Acta, 491, pp. 137-149. , 1:CAS:528:DyaE2sXhvVSiuro%3D 191085
  • Lama, A., Pawaria, S., Bidon-Chanal, A., Anand, A., Gelpí, J.L., Arya, S., Martí, M., Dikshit, K.L., (2009) J Biol Chem, 284, pp. 14457-14468. , 1:CAS:528:DC%2BD1MXlvV2isro%3D 10.1074/jbc.M807436200 19329431
  • Parrilli, E., Giuliani, M., Giordano, D., Russo, R., Marino, G., Verde, C., Tutino, M.L., (2010) Biochimie, 92, pp. 1003-1009. , 1:CAS:528:DC%2BC3cXovFyltLk%3D 10.1016/j.biochi.2010.04.018 20434514
  • Coletta, M., Angeletti, M., De Sanctis, G., Cerroni, L., Giardina, B., Amiconi, G., Ascenzi, P., (1996) Eur J Biochem, 235, pp. 49-53. , 1:CAS:528:DyaK28Xotlajsw%3D%3D 10.1111/j.1432-1033.1996.00049.x 8631366
  • De Sanctis, G., Petrella, G., Ciaccio, C., Feis, A., Smulevich, G., Coletta, M., A comparative study on axial coordination and ligand binding in ferric mini myoglobin and horse heart myoglobin (2007) Biophysical Journal, 93 (6), pp. 2135-2142. , http://www.biophysj.org/cgi/reprint/93/6/2135, DOI 10.1529/biophysj.106.098764
  • Watts, R.A., Hunt, P.W., Hvitved, A.N., Hargrove, M.S., Peacock, W.J., Dennis, E.S., A hemoglobin from plants homologous to truncated hemoglobins of microorganisms (2001) Proceedings of the National Academy of Sciences of the United States of America, 98 (18), pp. 10119-10124. , DOI 10.1073/pnas.191349198
  • Dewilde, S., Ebner, B., Vinck, E., Gilany, K., Hankeln, T., Burmester, T., Kreiling, J., Moens, L., The nerve hemoglobin of the bivalve mollusc Spisula solidissima: Molecular cloning, ligand binding studies, and phylogenetic analysis (2006) Journal of Biological Chemistry, 281 (9), pp. 5364-5372. , http://www.jbc.org/cgi/reprint/281/9/5364, DOI 10.1074/jbc.M509486200
  • Pesce, A., Dewilde, S., Nardini, M., Moens, L., Ascenzi, P., Hankeln, T., Burmester, T., Bolognesi, M., The human brain hexacoordinated neuroglobin three-dimensional structure (2004) Micron, 35 (1-2), pp. 63-65. , DOI 10.1016/j.micron.2003.10.013
  • Visca, P., Fabozzi, G., Petrucca, A., Ciaccio, C., Coletta, M., De Sanctis, G., Bolognesi, M., Ascenzi, P., The truncated hemoglobin from Mycobacterium lepraeq (2002) Biochemical and Biophysical Research Communications, 294 (5), pp. 1064-1070. , DOI 10.1016/S0006-291X(02)00593-4, PII S0006291X02005934
  • Scott, N.L., Falzone, C.J., Vuletich, D.A., Zhao, J., Bryant, D.A., Lecomte, J.T.J., Truncated hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002: Evidence for hexacoordination and covalent adduct formation in the ferric recombinant protein (2002) Biochemistry, 41 (22), pp. 6902-6910. , DOI 10.1021/bi025609m
  • Falzone, C.J., Vu, B.C., Scott, N.L., Lecomte, J.T.J., The solution structure of the recombinant hemoglobin from the cyanobacterium Synechocystis sp. PCC 6803 in its hemichrome state (2002) Journal of Molecular Biology, 324 (5), pp. 1015-1029. , DOI 10.1016/S0022-2836(02)01093-8
  • Razzera, G., Vernal, J., Baruh, D., Serpa, V.I., Tavares, C., Lara, F., Souza, E.M., Valente, A.P., (2008) J Biol Inorg Chem, 13, pp. 1085-1096. , 1:CAS:528:DC%2BD1cXhtFOqsLrJ 10.1007/s00775-008-0394-3 18548291
  • Burmester, T., Weich, B., Reinhardt, S., Hankeln, T., (2000) Nature, 407, pp. 520-523. , 1:STN:280:DC%2BD3cvnslKgtg%3D%3D 10.1038/35035093 11029004
  • Burmester, T., Ebner, B., Weich, B., Hankeln, T., (2002) Mol Biol Evol, 19, pp. 416-421. , 1:CAS:528:DC%2BD38XivV2gtLo%3D 11919282
  • Sowa, A.W., Guy, P.A., Sowa, S., Hill, R.D., (1999) Acta Biochim Pol, 46, pp. 431-445. , 1:CAS:528:DyaK1MXmt12gtLs%3D 10547043
  • Hargrove, M.S., Brucker, E.A., Stec, B., Sarath, G., Arredondo-Peter, R., Klucas, R.V., Olson, J.S., Phillips, G.N., (2000) Structure, 8, pp. 1005-1014. , 1:CAS:528:DC%2BD3cXmtlOktbc%3D 10.1016/S0969-2126(00)00194-5 10986467
  • Kriegl, J.M., Bhattacharyya, A.J., Nienhaus, K., Deng, P., Minkow, O., Nienhaus, G.U., Ligand binding and protein dynamics in neuroglobin (2002) Proceedings of the National Academy of Sciences of the United States of America, 99 (12), pp. 7992-7997. , DOI 10.1073/pnas.082244399
  • Smagghe, B.J., Trent III, J.T., Hargrove, M.S., NO dioxygenase activity in hemoglobins is ubiquitous in vitro, but limited by reduction in vivo (2008) PLoS ONE, 3 (4), pp. e2039. , http://www.plosone.org/article/fetchObjectAttachment.action?uri= info%3Adoi%2F10.1371%2Fjournal.pone.0002039&representation=PDF, DOI 10.1371/journal.pone.0002039

Citas:

---------- APA ----------
Howes, B.D., Giordano, D., Boechi, L., Russo, R., Mucciacciaro, S., Ciaccio, C., Sinibaldi, F.,..., Smulevich, G. (2011) . The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125. Journal of Biological Inorganic Chemistry, 16(2), 299-311.
http://dx.doi.org/10.1007/s00775-010-0726-y
---------- CHICAGO ----------
Howes, B.D., Giordano, D., Boechi, L., Russo, R., Mucciacciaro, S., Ciaccio, C., et al. "The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125" . Journal of Biological Inorganic Chemistry 16, no. 2 (2011) : 299-311.
http://dx.doi.org/10.1007/s00775-010-0726-y
---------- MLA ----------
Howes, B.D., Giordano, D., Boechi, L., Russo, R., Mucciacciaro, S., Ciaccio, C., et al. "The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125" . Journal of Biological Inorganic Chemistry, vol. 16, no. 2, 2011, pp. 299-311.
http://dx.doi.org/10.1007/s00775-010-0726-y
---------- VANCOUVER ----------
Howes, B.D., Giordano, D., Boechi, L., Russo, R., Mucciacciaro, S., Ciaccio, C., et al. The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125. J. Biol. Inorg. Chem. 2011;16(2):299-311.
http://dx.doi.org/10.1007/s00775-010-0726-y