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Volumn 53, Issue 5, 2012, Pages 1209-1210

Is the flavohemoglobin a nitric oxide dioxygenase?

Author keywords

[No Author keywords available]

Indexed keywords

DIOXYGENASE; ENZYME; FERRIC ION; FERROUS ION; FLAVOHEMOGLOBIN; HEMOGLOBIN; NITRIC OXIDE; NITRIC OXIDE DENITROSYLASE; NITRIC OXIDE DIOXYGENASE; NITRIC OXIDE REDUCTASE; UNCLASSIFIED DRUG;

EID: 84865484400     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2012.06.033     Document Type: Letter
Times cited : (13)

References (17)
  • 1
    • 84858964958 scopus 로고    scopus 로고
    • Protection from nitrosative stress: A central role for microbial flavohemoglobin
    • M.T. Forrester, and M.W. Foster Protection from nitrosative stress: a central role for microbial flavohemoglobin Free Radic. Biol. Med. 52 2012 1620 1633
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 1620-1633
    • Forrester, M.T.1    Foster, M.W.2
  • 2
    • 0034724887 scopus 로고    scopus 로고
    • Steady-state and transient kinetics of Escherichia coli nitric-oxide dioxygenase (flavohemoglobin): The B10 tyrosine hydroxyl is essential for dioxygen binding and catalysis
    • A.M. Gardner, L.A. Martin, P.R. Gardner, Y. Dou, and J.S. Olson Steady-state and transient kinetics of Escherichia coli nitric-oxide dioxygenase (flavohemoglobin): the B10 tyrosine hydroxyl is essential for dioxygen binding and catalysis J. Biol. Chem. 275 2000 12581 12589
    • (2000) J. Biol. Chem. , vol.275 , pp. 12581-12589
    • Gardner, A.M.1    Martin, L.A.2    Gardner, P.R.3    Dou, Y.4    Olson, J.S.5
  • 3
    • 84858734045 scopus 로고    scopus 로고
    • Real-time determination of intracellular oxygen in bacteria using a genetically encoded FRET-based biosensor
    • J. Potzkei, M. Kunze, T. Drepper, T. Gensch, K.E. Jaeger, and J. Buechs Real-time determination of intracellular oxygen in bacteria using a genetically encoded FRET-based biosensor BMC Biol. 10 2012 28
    • (2012) BMC Biol. , vol.10 , pp. 28
    • Potzkei, J.1    Kunze, M.2    Drepper, T.3    Gensch, T.4    Jaeger, K.E.5    Buechs, J.6
  • 5
    • 33644895690 scopus 로고    scopus 로고
    • Flavohemoglobin requires microaerophilic conditions for nitrosative protection of staphylococcus aureus
    • V.L. Goncalves, L.S. Nobre, J.B. Vicente, M. Teixeira, and L.M. Saraiva Flavohemoglobin requires microaerophilic conditions for nitrosative protection of staphylococcus aureus FEBS Lett 580 2006 1817 1821
    • (2006) FEBS Lett , vol.580 , pp. 1817-1821
    • Goncalves, V.L.1    Nobre, L.S.2    Vicente, J.B.3    Teixeira, M.4    Saraiva, L.M.5
  • 6
    • 33748801201 scopus 로고    scopus 로고
    • Maintenance of nitric oxide and redox homeostasis by the Salmonella flavohemoglobin hmp
    • I.S. Bang, L. Liu, A. Vazquez-Torres, M.L. Crouch, J.S. Stamler, and F.C. Fang Maintenance of nitric oxide and redox homeostasis by the Salmonella flavohemoglobin hmp J. Biol. Chem. 281 2006 28039 28047
    • (2006) J. Biol. Chem. , vol.281 , pp. 28039-28047
    • Bang, I.S.1    Liu, L.2    Vazquez-Torres, A.3    Crouch, M.L.4    Stamler, J.S.5    Fang, F.C.6
  • 7
    • 33749016490 scopus 로고    scopus 로고
    • Essential role of flavohemoglobin in long-term anaerobic survival of Bacillus subtilis
    • M.M. Nakano Essential role of flavohemoglobin in long-term anaerobic survival of Bacillus subtilis J. Bacteriol 188 2006 6415 6418
    • (2006) J. Bacteriol , vol.188 , pp. 6415-6418
    • Nakano, M.M.1
  • 8
    • 84860176878 scopus 로고    scopus 로고
    • Endogenous protein S-nitrosylation in E. coli: Regulation by OxyR
    • D. Seth, A. Hausladen, Y.J. Wang, and J.S. Stamler Endogenous protein S-nitrosylation in E. coli: regulation by OxyR Science 336 2012 470 473
    • (2012) Science , vol.336 , pp. 470-473
    • Seth, D.1    Hausladen, A.2    Wang, Y.J.3    Stamler, J.S.4
  • 9
    • 0035964364 scopus 로고    scopus 로고
    • Flavohemoglobin denitrosylase catalyzes the reaction of a nitroxyl equivalent with molecular oxygen
    • A. Hausladen, A. Gow, and J.S. Stamler Flavohemoglobin denitrosylase catalyzes the reaction of a nitroxyl equivalent with molecular oxygen Proc. Natl. Acad. Sci. USA 98 2001 10108 10112
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10108-10112
    • Hausladen, A.1    Gow, A.2    Stamler, J.S.3
  • 10
    • 0035863151 scopus 로고    scopus 로고
    • Escherichia coli flavohaemoglobin (hmp) with equistoichiometric FAD and haem contents has a low affinity for dioxygen in the absence or presence of nitric oxide
    • C.E. Mills, S. Sedelnikova, B. Soballe, M.N. Hughes, and R.K. Poole Escherichia coli flavohaemoglobin (hmp) with equistoichiometric FAD and haem contents has a low affinity for dioxygen in the absence or presence of nitric oxide Biochem. J 353 2001 207 213
    • (2001) Biochem. J , vol.353 , pp. 207-213
    • Mills, C.E.1    Sedelnikova, S.2    Soballe, B.3    Hughes, M.N.4    Poole, R.K.5
  • 11
    • 0035831479 scopus 로고    scopus 로고
    • Flavohemoglobin, a globin with a peroxidase-like catalytic site
    • M. Mukai, C.E. Mills, R.K. Poole, and S.R. Yeh Flavohemoglobin, a globin with a peroxidase-like catalytic site J. Biol. Chem. 276 2001 7272 7277
    • (2001) J. Biol. Chem. , vol.276 , pp. 7272-7277
    • Mukai, M.1    Mills, C.E.2    Poole, R.K.3    Yeh, S.R.4
  • 12
    • 0023274482 scopus 로고
    • Reaction of nitric oxide with heme proteins and model compounds of hemoglobin
    • V.S. Sharma, T.G. Traylor, R. Gardiner, and H. Mizukami Reaction of nitric oxide with heme proteins and model compounds of hemoglobin Biochemistry 2 6 1987 3837 3843
    • (1987) Biochemistry , vol.2 , Issue.6 , pp. 3837-3843
    • Sharma, V.S.1    Traylor, T.G.2    Gardiner, R.3    Mizukami, H.4
  • 14
    • 80051551027 scopus 로고    scopus 로고
    • Globin-mediated nitric oxide detoxification in the foodborne pathogenic bacterium Campylobacter jejuni proceeds via a dioxygenase or denitrosylase mechanism
    • M. Shepherd, P.V. Bernhardt, and R.K. Poole Globin-mediated nitric oxide detoxification in the foodborne pathogenic bacterium Campylobacter jejuni proceeds via a dioxygenase or denitrosylase mechanism Nitric Oxide 25 2011 229 233
    • (2011) Nitric Oxide , vol.25 , pp. 229-233
    • Shepherd, M.1    Bernhardt, P.V.2    Poole, R.K.3
  • 15
    • 0029610660 scopus 로고
    • Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution
    • U. Ermler, R.A. Siddiqui, R. Cramm, and B. Friedrich Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution EMBO J 14 1995 6067 6077
    • (1995) EMBO J , vol.14 , pp. 6067-6077
    • Ermler, U.1    Siddiqui, R.A.2    Cramm, R.3    Friedrich, B.4
  • 17
    • 13244299310 scopus 로고    scopus 로고
    • New genes implicated in the protection of anaerobically grown Escherichia coli against nitric oxide
    • M.C. Justino, J.B. Vicente, M. Teixeira, and L.M. Saraiva New genes implicated in the protection of anaerobically grown Escherichia coli against nitric oxide J. Biol. Chem. 280 2005 2636 2643
    • (2005) J. Biol. Chem. , vol.280 , pp. 2636-2643
    • Justino, M.C.1    Vicente, J.B.2    Teixeira, M.3    Saraiva, L.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.