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Volumn 122, Issue 33, 2000, Pages 7869-7875

ENDOR spectroscopic evidence for the geometry of binding of retro-inverso-N(ω)-nitroarginine-containing dipeptide amides to neuronal nitric oxide synthase

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE; DIPEPTIDE; N(G) NITROARGININE; NITRIC OXIDE SYNTHASE;

EID: 0034706017     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja993927b     Document Type: Article
Times cited : (15)

References (35)
  • 8
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    • Garthwaite, J. in The NMDA Receptor; Watkins, J. C., Collingridge, G. L., Eds.; Oxford University Press: Oxford, England, 1989; pp 187-205.
    • (1989) The NMDA Receptor , pp. 187-205
    • Garthwaite, J.1
  • 16
    • 0000389187 scopus 로고
    • Berliner, L. J., Reuben, J., Eds.; Metalloenzyme Active-Site Structure and Function through Multifrequency CW and Pulsed ENDOR, Plenum Press: New York and London
    • Hoffman, B. M.; DeRose, V. J.; Doan, P. E.; Gurbiel, R. J.; Houseman, A. L. P.; Telser, J. Biological Magnetic Resonance; Berliner, L. J., Reuben, J., Eds.; Metalloenzyme Active-Site Structure and Function through Multifrequency CW and Pulsed ENDOR, Vol. 13; Plenum Press: New York and London, 1993; pp 151-218.
    • (1993) Biological Magnetic Resonance , vol.13 , pp. 151-218
    • Hoffman, B.M.1    DeRose, V.J.2    Doan, P.E.3    Gurbiel, R.J.4    Houseman, A.L.P.5    Telser, J.6
  • 17
    • 0028963868 scopus 로고
    • Sauer, K., Ed.; Protein Structure and Mechanism Studied by Electron Nuclear Double Resonance Spectroscopy, Academic Press: New York
    • DeRose, V. J.; Hoffman, B. M. Methods in Enzymology; Sauer, K., Ed.; Protein Structure and Mechanism Studied by Electron Nuclear Double Resonance Spectroscopy, Vol. 246; Academic Press: New York, 1995; pp 554-589.
    • (1995) Methods in Enzymology , vol.246 , pp. 554-589
    • DeRose, V.J.1    Hoffman, B.M.2
  • 22
    • 0342549089 scopus 로고    scopus 로고
    • note
    • A recent low-resolution (2.6 Å) crystal structure of the iNOS oxygenase domain complexed with NOHA showed that the N of the NOHA "N-OH" moiety is roughly above the heme Fe, thereby leading to the ENDOR-based conclusion that this is, in fact, an "NH-OH" moiety.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.