1buw Citations

Crystal structure of the S-nitroso form of liganded human hemoglobin.

Biochemistry 37 16459-64 (1998)
Cited: 65 times
EuropePMC logo PMID: 9843411

Abstract

Although numerous reports have documented that the S-nitrosylation of cysteine residues by NO alters the activities of a wide variety of proteins, the direct visualization and the structural consequences of this reversible modification have not yet been reported for any protein. Here we describe the crystal structure of S-nitroso-nitrosylhemoglobin determined at a resolution of 1.8 A. The specific reaction of NO with Cys93beta is confirmed in this structure, and a large S-nitrosylation-induced change in the tertiary structure of the COOH-terminal dipeptides of the beta subunits provides additional insight into the stereochemical mechanism by which blood flow is regulated by the interaction of NO with hemoglobin.

Reviews - 1buw mentioned but not cited (1)

  1. NO and Heme Proteins: Cross-Talk between Heme and Cysteine Residues. Verde C, Giordano D, Bruno S. Antioxidants (Basel) 12 321 (2023)

Articles - 1buw mentioned but not cited (8)



Reviews citing this publication (20)

  1. Chemical physiology of blood flow regulation by red blood cells: the role of nitric oxide and S-nitrosohemoglobin. Singel DJ, Stamler JS. Annu Rev Physiol 67 99-145 (2005)
  2. Protein S-Nitrosylation: Determinants of Specificity and Enzymatic Regulation of S-Nitrosothiol-Based Signaling. Stomberski CT, Hess DT, Stamler JS. Antioxid Redox Signal 30 1331-1351 (2019)
  3. Heme-based sensors in biological systems. Rodgers KR. Curr Opin Chem Biol 3 158-167 (1999)
  4. The decomposition of thionitrites. Stamler JS, Toone EJ. Curr Opin Chem Biol 6 779-785 (2002)
  5. Biochemical aspects of the reaction of hemoglobin and NO: implications for Hb-based blood substitutes. Patel RP. Free Radic Biol Med 28 1518-1525 (2000)
  6. Effect of processing and storage on red blood cell function in vivo. Doctor A, Spinella P. Semin Perinatol 36 248-259 (2012)
  7. Role of Nitric Oxide Carried by Hemoglobin in Cardiovascular Physiology: Developments on a Three-Gas Respiratory Cycle. Premont RT, Reynolds JD, Zhang R, Stamler JS. Circ Res 126 129-158 (2020)
  8. Effect of diet and gut environment on the gastrointestinal formation of N-nitroso compounds: A review. Kobayashi J. Nitric Oxide 73 66-73 (2018)
  9. Measurement of 3-nitrotyrosine and 5-nitro-gamma-tocopherol by high-performance liquid chromatography with electrochemical detection. Hensley K, Williamson KS, Floyd RA. Free Radic Biol Med 28 520-528 (2000)
  10. Transport and peripheral bioactivities of nitrogen oxides carried by red blood cell hemoglobin: role in oxygen delivery. Sonveaux P, Lobysheva II, Feron O, McMahon TJ. Physiology (Bethesda) 22 97-112 (2007)
  11. Methodologies for the characterization, identification and quantification of S-nitrosylated proteins. Foster MW. Biochim Biophys Acta 1820 675-683 (2012)
  12. Computational Structural Biology of S-nitrosylation of Cancer Targets. Bignon E, Allega MF, Lucchetta M, Tiberti M, Papaleo E. Front Oncol 8 272 (2018)
  13. Distribution, adaptation and physiological meaning of thiols from vertebrate hemoglobins. Reischl E, Dafre AL, Franco JL, Wilhelm Filho D. Comp Biochem Physiol C Toxicol Pharmacol 146 22-53 (2007)
  14. S-Nitrosohemoglobin: an allosteric mediator of NO group function in mammalian vasculature. Frehm EJ, Bonaventura J, Gow AJ. Free Radic Biol Med 37 442-453 (2004)
  15. Red Blood Cell-Mediated S-Nitrosohemoglobin-Dependent Vasodilation: Lessons Learned from a β-Globin Cys93 Knock-In Mouse. Premont RT, Reynolds JD, Zhang R, Stamler JS. Antioxid Redox Signal 34 936-961 (2021)
  16. The enzymatic function of the honorary enzyme: S-nitrosylation of hemoglobin in physiology and medicine. Premont RT, Singel DJ, Stamler JS. Mol Aspects Med 84 101056 (2022)
  17. Chemical regulation of nitric oxide: a role for intracellular myoglobin? Andriambeloson E, Witting PK. Redox Rep 7 131-136 (2002)
  18. Red Blood Cell Dysfunction in Critical Illness. Rogers S, Doctor A. Crit Care Clin 36 267-292 (2020)
  19. Red cell physiology and signaling relevant to the critical care setting. Said A, Rogers S, Doctor A. Curr Opin Pediatr 27 267-276 (2015)
  20. Protein S-Nitrosylation: A Chemical Modification with Ubiquitous Biological Activities. Aboalroub AA, Al Azzam KM. Protein J 43 639-655 (2024)

Articles citing this publication (36)