Redox chemistry and chemical biology of H2S, hydropersulfides, and derived species: Implications of their possible biological activity and utility
Open accessAbstract
Hydrogen sulfide (H2S) is an endogenously generated and putative signaling/effector molecule. Despite its numerous reported functions, the chemistry by which it elicits its functions is not understood. Moreover, recent studies allude to the existence of other sulfur species besides H2S that may play critical physiological roles. Herein, the basic chemical biology of H2S as well as other related or derived species is discussed and reviewed. This review particularly focuses on the per- and polysulfides which are likely in equilibrium with free H2S and which may be important biological effectors themselves.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
NO, CO and H2S differ in potency and appear to mediate their biological action via different signaling pathways, but their action spectrum shows remarkable overlap.
“Although this recognition lacks universal agreement [6,7], and the three molecules differ in potency and appear to mediate their biological action via different signaling pathways, their action spectrum shows remarkable overlap.”
From On the chemical biology of the nitrite/sulfide interaction (2015) · cites this paper as [7]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
The Pecking Order of Free Radicals and Antioxidants: Lipid Peroxidation, α-Tocopherol, and Ascorbate
Buettner, G. R. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1074 · Cited by 2,417 · see citing works
Physiological Implications of Hydrogen Sulfide: A Whiff Exploration That Blossomed
Wang, R. (2012) · Physiological Reviews · doi:10.1152/physrev.00017.2011 · Cited by 1,939 · see citing works
Protein Radicals in Enzyme Catalysis
Stubbe, J., & van der Donk, W. A. (1998) · Chemical Reviews · doi:10.1021/cr9400875 · Cited by 1,378 · see citing works
H 2 S Signals Through Protein S-Sulfhydration
Mustafa, A. K., Gadalla, M. M., Sen, N., Kim, S., Mu, W., Gazi, S. K., Barrow, R. K., Yang, G., Wang, R., & Snyder, S. H. (2009) · Science Signaling · doi:10.1126/scisignal.2000464 · Cited by 1,235 · see citing works
Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling
Ida, T., Sawa, T., Ihara, H., Tsuchiya, Y., Watanabe, Y., Kumagai, Y., Suematsu, M., Motohashi, H., Fujii, S., Matsunaga, T., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321232111 · Cited by 934 · see citing works
Self-citationH 2 S Induces a Suspended Animation-Like State in Mice
Blackstone, E., Morrison, M., & Roth, M. B. (2005) · Science · doi:10.1126/science.1108581 · Cited by 802 · see citing works
Sulfur and Selenium: The Role of Oxidation State in Protein Structure and Function
Jacob, C., Giles, G. I., Giles, N. M., & Sies, H. (2003) · Angewandte Chemie International Edition · doi:10.1002/anie.200300573 · Cited by 757 · see citing works
Redox Biochemistry of Hydrogen Sulfide
Kabil, Ö., & Banerjee, R. V. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.128363 · Cited by 745 · see citing works
Cooper, C. E., & Brown, G. C. (2008) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-008-9166-6 · Cited by 724 · see citing works
The Factors Determining Nucleophilic Reactivities
Edwards, J. O., & Pearson, R. G. (1962) · Journal of the American Chemical Society · doi:10.1021/ja00860a005 · Cited by 707 · see citing works
Thermochemistry and kinetics of sulfur-containing molecules and radicals
Benson, S. W. (1978) · Chemical Reviews · doi:10.1021/cr60311a003 · Cited by 706 · see citing works
Reduction Potentials Involving Inorganic Free Radicals in Aqueous Solution
Stanbury, D. M. (1989) · Advances in inorganic chemistry · doi:10.1016/s0898-8838(08)60194-4 · Cited by 656 · see citing works
Hydrogen sulfide: its production, release and functions
Kimura, H. (2010) · Amino Acids · doi:10.1007/s00726-010-0510-x · Cited by 635 · see citing works
Furne, J. K., Saeed, A., & Levitt, M. D. (2008) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.90566.2008 · Cited by 628 · see citing works
Conrad, M., & Sato, H. (2011) · Amino Acids · doi:10.1007/s00726-011-0867-5 · Cited by 607 · see citing works
Exchange of cystine and glutamate across plasma membrane of human fibroblasts.
Bannai, S. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35926-4 · Cited by 543 · see citing works
Mustafa, A. K., Gadalla, M. M., & Snyder, S. H. (2009) · Science Signaling · doi:10.1126/scisignal.268re2 · Cited by 491 · see citing works
Nagy, P. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4973 · Cited by 488 · see citing works
Self-citationHydrogen sulfide chemical biology: pathophysiological roles and detection
Kolluru, G. K., Shen, X., Bir, S. C., & Kevil, C. G. (2013) · Nitric Oxide · doi:10.1016/j.niox.2013.07.002 · Cited by 480 · see citing works
Polysulfides Link H 2 S to Protein Thiol Oxidation
Greiner, R., Pálinkás, Z., Bäsell, K., Becher, D., Antelmann, H., Nagy, P., & Dick, T. P. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5041 · Cited by 471 · see citing works
Self-citationThe Biological Chemistry of Hydrogen Peroxide
Winterbourn, C. C. (2013) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-405881-1.00001-x · Cited by 459 · see citing works
Transport interaction of L-cystine and L-glutamate in human diploid fibroblasts in culture.
Bannai, S., & Kitamura, E. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85901-x · Cited by 456 · see citing works
Krishnan, N., Fu, C., Pappin, D., & Tonks, N. K. (2011) · Science Signaling · doi:10.1126/scisignal.2002329 · Cited by 447 · see citing works
Szabó, C., Ransy, C., Módis, K., Andriamihaja, M., Murghes, B., Coletta, C., Oláh, G., Yanagi, K., & Bouillaud, F. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12369 · Cited by 440 · see citing works
Sulfide, the first inorganic substrate for human cells
Goubern, M., Andriamihaja, M., Nübel, T., Blachier, F., & Bouillaud, F. (2007) · The FASEB Journal · doi:10.1096/fj.06-7407com · Cited by 424 · see citing works
Redox imbalance in cystine/glutamate transporter-deficient mice
Sato, H., Shiiya, A., Kimata, M., Maebara, K., Tamba, M., Sakakura, Y., Makino, N., Sugiyama, F., Yagami, K.-I., Moriguchi, T., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506439200 · Cited by 422 · see citing works
Humphries, J. D., Byron, A., Bass, M. D., Craig, S. E., Pinney, J. W., Knight, D., & Humphries, M. J. (2009) · Science Signaling · doi:10.1126/scisignal.2000396 · Cited by 404 · see citing works
Tiranti, V., Viscomi, C. F., Hildebrandt, T. M., Meo, I. D., Mineri, R., Tiveron, C., Levitt, M. D., Prelle, A. C., Fagiolari, G., Rimoldi, M., et al. (2009) · Nature Medicine · doi:10.1038/nm.1907 · Cited by 404 · see citing works
EXTRACELLULAR THIOLS AND THIOL/DISULFIDE REDOX IN METABOLISM
Moriarty-Craige, S. E., & Jones, D. P. (2004) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.24.012003.132208 · Cited by 390 · see citing works
Fukuto, J. M., Carrington, S. J., Tantillo, D. J., Harrison, J. G., Ignarro, L. J., Freeman, B. A., Chen, A., & Wink, D. A. (2012) · Chemical Research in Toxicology · doi:10.1021/tx2005234 · Cited by 389 · see citing works
Metabolism of Sulfur-Containing Amino Acids
Stipanuk, M. H. (1986) · Annual Review of Nutrition · doi:10.1146/annurev.nu.06.070186.001143 · Cited by 385 · see citing works
On the Mechanism of Inactivation of Xanthine Oxidase by Cyanide
Massey, V., & Edmondson, D. E. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62575-x · Cited by 368 · see citing works
Dorman, D. C. (2002) · Toxicological Sciences · doi:10.1093/toxsci/65.1.18 · Cited by 362 · see citing works
Traylor, T. G., & Sharma, V. S. (1992) · Biochemistry · doi:10.1021/bi00126a001 · Cited by 354 · see citing works
Chemical foundations of hydrogen sulfide biology
Li, Q., & Lancaster, J. R. (2013) · Nitric Oxide · doi:10.1016/j.niox.2013.07.001 · Cited by 334 · see citing works
Measurement of plasma hydrogen sulfide in vivo and in vitro
Shen, X., Pattillo, C. B., Pardue, S., Bir, S. C., Wang, R., & Kevil, C. G. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.01.025 · Cited by 325 · see citing works
Biology and therapeutic potential of hydrogen sulfide and hydrogen sulfide-releasing chimeras
Kashfi, K., & Olson, K. R. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.10.019 · Cited by 315 · see citing works
Metabolism of Sulfur-Containing Amino Acids
Stipanuk, M. H. (1986) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.6.1.179 · Cited by 304 · see citing works
Jones, D. P., Go, Y., Anderson, C. L., Ziegler, T. R., Kinkade, J. M., & Kirlin, W. G. (2004) · The FASEB Journal · doi:10.1096/fj.03-0971fje · Cited by 302 · see citing works
Jackson, M. R. C., Melideo, S. L., & Jörns, M. S. (2012) · Biochemistry · doi:10.1021/bi300778t · Cited by 291 · see citing works
Detection of Protein S‐Sulfhydration by a Tag‐Switch Technique
Zhang, D., Mačinković, I., Devarie‐Baez, N. O., Pan, J. H., Park, C., Carroll, K. S., Filipović, M. R., & Xian, M. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201305876 · Cited by 289 · see citing works
Self-citationMultiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis
Morgan, B., Ezeriņa, D., Amoako, T. N. E., Riemer, J., Seedorf, M., & Dick, T. P. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1142 · Cited by 288 · see citing works
Chemical aspects of hydrogen sulfide measurements in physiological samples
Nagy, P., Pálinkás, Z., Nagy, A., Budai, B., Tóth, I., & Vasas, A. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.05.037 · Cited by 285 · see citing works
Self-citationSulfur signaling: Is the agent sulfide or sulfane?
Toohey, J. I. (2011) · Analytical Biochemistry · doi:10.1016/j.ab.2011.01.044 · Cited by 276 · see citing works
Antibody Catalysis of the Oxidation of Water
Wentworth, P., Jones, L. H., Wentworth, A. D., et al. (2001) · Science · doi:10.1126/science.1062722 · Cited by 267 · see citing works
Kajimura, M., Fukuda, R., Bateman, R. M., Yamamoto, T., & Suematsu, M. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2657 · Cited by 265 · see citing works
Whiteman, M., & Moore, P. K. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00645.x · Cited by 261 · see citing works
Sulphane sulphur in biological systems: a possible regulatory role
Toohey, J. I. (1989) · Biochemical Journal · doi:10.1042/bj2640625 · Cited by 246 · see citing works
H2S and its role in redox signaling
Kabil, O., Motl, N., & Banerjee, R. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.01.002 · Cited by 240 · see citing works
AKT Promotes rRNA Synthesis and Cooperates with c-MYC to Stimulate Ribosome Biogenesis in Cancer
Chan, J. C., Hannan, K. M., Riddell, K., Ng, P. Y., Peck, A., Lee, R. S., Hung, S. S. C., Astle, M. V., Bywater, M. J., Wall, M., et al. (2011) · Science Signaling · doi:10.1126/scisignal.2001754 · Cited by 239 · see citing works
SUSPENDED ANIMATION-LIKE STATE PROTECTS MICE FROM LETHAL HYPOXIA
Blackstone, E., & Roth, M. B. (2007) · Shock · doi:10.1097/shk.0b013e31802e27a0 · Cited by 238 · see citing works
New fluorescent probes for sulfane sulfurs and the application in bioimaging
Chen, W., Liu, C., Peng, B., Zhao, Y., Pacheco, A., & Xian, M. (2013) · Chemical Science · doi:10.1039/c3sc50754h · Cited by 223 · see citing works
Self-citationPolysulfides as biologically active ingredients of garlic
Münchberg, U., Anwar, A., Mecklenburg, S., & Jacob, C. (2007) · Organic & Biomolecular Chemistry · doi:10.1039/b703832a · Cited by 219 · see citing works
Nagy, P., & Winterbourn, C. C. (2010) · Chemical Research in Toxicology · doi:10.1021/tx100266a · Cited by 213 · see citing works
Self-citationHydrogen Sulfide and Hemeproteins: Knowledge and Mysteries
Pietri, R. B., Román-Morales, E., & Lopez-Garriga, J. J. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3698 · Cited by 208 · see citing works
The reaction of H2S with oxidized thiols: generation of persulfides and implications to H2S biology
Francoleon, N. E., Carrington, S. J., & Fukuto, J. M. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.09.015 · Cited by 199 · see citing works
Self-citationKraus, D. W., & Wittenberg, J. B. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46185-0 · Cited by 191 · see citing works
Persulfide Reactivity in the Detection of Protein S-Sulfhydration
Pan, J. H., & Carroll, K. S. (2013) · ACS Chemical Biology · doi:10.1021/cb4001052 · Cited by 187 · see citing works
Hydrogen Sulfide Oxidation Is Coupled to Oxidative Phosphorylation in Mitochondria of Solemya reidi
Powell, M. A., & Somero, G. N. (1986) · Science · doi:10.1126/science.233.4763.563 · Cited by 174 · see citing works
Microbial Transsulfuration: the Mechanism of an Enzymatic Disulfide Elimination Reaction
Flavin, M. (1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60371-0 · Cited by 164 · see citing works
Kinetics and mechanism of oxidation of hydrogen sulfide by hydrogen peroxide in acidic solution
Hoffmann, M. R. (1977) · Environmental Science & Technology · doi:10.1021/es60124a004 · Cited by 160 · see citing works
Collman, J. P., Dey, S. G., Dey, A., & Decréau, R. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904082106 · Cited by 159 · see citing works
Reduction potentials and exchange reactions of thiyl radicals and disulfide anion radicals
Surdhar, P. S., & Armstrong, D. A. (1987) · The Journal of Physical Chemistry · doi:10.1021/j100310a022 · Cited by 159 · see citing works
Kabil, Ö., & Banerjee, R. V. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.407411 · Cited by 156 · see citing works
Cystine uptake and glutathione level in endothelial cells exposed to oxidative stress
Miura, K., Ishii, T., Sugita, Y., et al. (1992) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1992.262.1.c50 · Cited by 146 · see citing works
Munday, R., Munday, J. S., & Munday, C. M. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00144-8 · Cited by 143 · see citing works
Redox Chemistry of Biological Thiols
Nagy, P., & Winterbourn, C. C. (2010) · Advances in molecular toxicology · doi:10.1016/s1872-0854(10)04006-3 · Cited by 125 · see citing works
Self-citationSulfide oxidation coupled to ATP synthesis in chicken liver mitochondria
Yong, R., & Searcy, D. G. (2001) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/s1096-4959(01)00309-8 · Cited by 125 · see citing works
Interactions of hydrogen sulfide with myeloperoxidase
Pálinkás, Z., Furtmüller, P. G., Nagy, A., Jakopitsch, C., Pirker, K. F., Magierowski, M., Jasnos, K., Wallace, J. L., Obinger, C., & Nagy, P. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12769 · Cited by 116 · see citing works
Self-citationFactors Controlling the Reactivity of Hydrogen Sulfide with Hemeproteins
Pietri, R. B., Lewis, A., León, R., Casabona, G., Kiger, L., Yeh, S., Fernández-Alberti, S., Marden, M. C., Cadilla, C. L., & Lopez-Garriga, J. J. (2009) · Biochemistry · doi:10.1021/bi801738j · Cited by 115 · see citing works
One- and two-electron reduction potentials of peroxyl radicals and related species
Merényi, G., Lind, J. U., & Engman, L. (1994) · Journal of the Chemical Society Perkin Transactions 2 · doi:10.1039/p29940002551 · Cited by 108 · see citing works
Redox potentials of some sulfur-containing radicals
Surdhar, P. S., & Armstrong, D. A. (1986) · The Journal of Physical Chemistry · doi:10.1021/j100280a091 · Cited by 105 · see citing works
Kraus, D. W., Wittenberg, J. B., Lu, J. F., & Peisach, J. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46186-2 · Cited by 97 · see citing works
Evidence for an Active Site Persulfide Residue in Rabbit Liver Aldehyde Oxidase
Branzoli, U., & Massey, V. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42426-5 · Cited by 94 · see citing works
Das, T. N., Huie, R. E., Neta, P., & Padmaja, S. (1999) · The Journal of Physical Chemistry A · doi:10.1021/jp9907544 · Cited by 92 · see citing works
Hydrogen sulfide activation in hemeproteins: The sulfheme scenario
Ríos-González, B. B., Román-Morales, E., Pietri, R. B., & Lopez-Garriga, J. J. (2014) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2014.01.013 · Cited by 88 · see citing works
Madej, E., & Wardman, P. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.03.002 · Cited by 87 · see citing works
Interaction of Proteins with Sulfide
Cavallini, D., Federici, G., & Barboni, E. (1970) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1970.tb00275.x · Cited by 86 · see citing works
Bolognesi, M., Rosano, C., Losso, R., et al. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)76959-6 · Cited by 84 · see citing works
[5] Perthiols as antioxidants: Radical-scavenging andprooxidative mechanisms
Everett, S. A., & Wardman, P. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)51110-5 · Cited by 80 · see citing works
The Mechanism of the L-Cystine Cleavage Reaction Catalyzed by Rat Liver γ-Cystathionase1
YAMANISHI, T., & Tuboi, S. (1981) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a133393 · Cited by 80 · see citing works
Structural Bases for Sulfide Recognition inLucina pectinataHemoglobin I
Rizzi, M., Wittenberg, J. B., Coda, A., Ascenzi, P., & Bolognesi, M. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0228 · Cited by 78 · see citing works
Steudel, R., Drozdova, Y. A., Mia̧skiewicz, K., et al. (1997) · Journal of the American Chemical Society · doi:10.1021/ja9624026 · Cited by 76 · see citing works
Hydrosulfide (HS−) Coordination in Iron Porphyrinates
Pavlik, J. W., Noll, B. C., Oliver, A. G., Schulz, C. E., & Scheidt, W. R. (2009) · Inorganic Chemistry · doi:10.1021/ic901853p · Cited by 76 · see citing works
On the combinations of methæmoglobin with H 2S
Keilin, D. (1933) · Proceedings of the Royal Society of London Series B Containing Papers of a Biological Character · doi:10.1098/rspb.1933.0056 · Cited by 74 · see citing works
Oxygen, oxysterols, ouabain, and ozone: a cautionary tale
Smith, L. L. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.04.024 · Cited by 72 · see citing works
Everett, S. A., Schöneich, C., Stewart, J. H., & Asmus, K. D. (1992) · The Journal of Physical Chemistry · doi:10.1021/j100180a058 · Cited by 70 · see citing works
Reaction of Cystine with Sodium Sulfide in Sodium Hydroxide Solution
Rao, G., & Gorin, G. (1959) · The Journal of Organic Chemistry · doi:10.1021/jo01088a005 · Cited by 66 · see citing works
xCT deficiency accelerates chemically induced tumorigenesis
Nabeyama, A., Kurita, A., Asano, K., Miyake, Y., Yasuda, T., Miura, I., Nishitai, G., Arakawa, S., Shimizu, S., Wakana, S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912827107 · Cited by 65 · see citing works
Marsden, C. J., & Smith, B. J. (1988) · The Journal of Physical Chemistry · doi:10.1021/j100313a021 · Cited by 60 · see citing works
Anderson, C. L., Iyer, S. S., Ziegler, T. R., & Jones, D. P. (2007) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00195.2007 · Cited by 59 · see citing works
Massey, V., Williams, C. H., & Palmer, G. (1971) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(71)90548-1 · Cited by 54 · see citing works
Bickelhaupt, F. M., Solà, M., & Schleyer, P. V. R. (1995) · Journal of Computational Chemistry · doi:10.1002/jcc.540160410 · Cited by 52 · see citing works
The interaction of human neuroglobin with hydrogen sulphide
Brittain, T., Yosaatmadja, Y., & Henty, K. (2008) · IUBMB Life · doi:10.1002/iub.16 · Cited by 48 · see citing works
Nguyen, B. D., Zhao, X., Vyas, K., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.9517 · Cited by 48 · see citing works
Cleavage of cystine by a pyridoxal model
Cavallinì, D., de Marco, C., & Mondovı̀, B. (1960) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(60)90173-9 · Cited by 45 · see citing works
Disulfide anion radical equilibria: effects of -NH3+, -CO2−, -NHC(O)- and -CH3 groups
Mezyk, S. P., & Armstrong, D. A. (1999) · Journal of the Chemical Society Perkin Transactions 2 · doi:10.1039/a901155b · Cited by 32 · see citing works
Shereshovets, V. V., Khursan, S. L., Komissarov, V. D., et al. (2001) · Russian Chemical Reviews · doi:10.1070/rc2001v070n02abeh000622 · Cited by 28 · see citing works
Thiosulfoxides (X2SS) and disulfanes (XSSX):
Gerbaux, P., Salpin, J., Bouchoux, G., et al. (2000) · International Journal of Mass Spectrometry · doi:10.1016/s1387-3806(99)00227-4 · Cited by 22 · see citing works
Boffi, A., Rizzi, M., Monacelli, F., et al. (2000) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(00)00123-9 · Cited by 21 · see citing works
Interactions of hydrogen sulfide with myeloperoxidase☆
Pálinkás, Z., Furtmüller, P. G., Nagy, A., et al. (2015) · Nitric Oxide · doi:10.1016/j.niox.2015.02.140 · Cited by 10 · see citing works
Hiskey, R. G., Bowers, W. H., & Harpp, D. N. (1964) · Journal of the American Chemical Society · doi:10.1021/ja01064a020 · Cited by 9 · see citing works
Inhibition of rat liver cytochrome P-450 by benzyl hydrodisulfide.
Sawahata, T., & Neal, R. A. (1982) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)14617-8 · Cited by 8 · see citing works
The Chemistry of Aliphatic Disulfides. III.1 Formation of Sulfides During Cleavage by Cyanide Ion2
Hiskey, R. G., & Carroll, F. I. (1961) · Journal of the American Chemical Society · doi:10.1021/ja01483a034 · Cited by 6 · see citing works
Flagged first, then by citations
Research works printed but not linked: 2
- [18]Keilin D On the combination of methaemoglobin with H2S Proc. Royal Soc. London, Series B, Containing papers of a Biological Nature 1933 113 393 404
- [69]Cavallini D Federici G Barboni E Interaction of proteins with sulfide Eur. J. Biochem 1970 14 169 174 5447431
Cited by
Sorted by citations
On the chemical biology of the nitrite/sulfide interaction
Cortese-Krott, M. M., Fernandez, B. O., Kelm, M., Butler, A. R., & Feelisch, M. (2015) · Nitric Oxide · doi:10.1016/j.niox.2014.12.009 · Cited by 115 · see citing works
- Authors
- Ono, K., Akaike, T., Sawa, T., Kumagai, Y., Wink, D. A., Tantillo, D. J., Hobbs, A. J., Nagy, P., Xian, M., Lin, J., & Fukuto, J. M.
- Affiliations
- Sonoma State University (US)
- Tohoku University (JP)
- University of Tsukuba (JP)
- National Institutes of Health (US)
- University of California, Davis (US)
- Queen Mary University of London (GB)
- Washington State University (US)
- Corresponding author
- Fukuto, Jon M.
- ORCID
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2014-12
- Volume
- 77
- Pages
- 82-94
- ISSN
- 0891-5849 (ISSN-L)
- PMC
- PMC4258476
- OpenAlex
- W2017521727
- Cited by
- 422
- References
- 105
- Citations by year
- 2026: 27 · 2025: 17 · 2024: 33 · 2023: 36 · 2022: 36 · 2021: 27 · 2020: 46 · 2019: 44 · 2018: 36 · 2017: 46 · 2016: 40 · 2015: 28 · 2014: 4 · 2013: 1
- FWCI
- 3.37
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Queen Mary Research Online (Queen Mary University of London) (submittedVersion)
- Funders
- Marie Curie International Reintegration (PIRG08-GA-2010-277006)
- The Hungarian National Science Foundation (K109843)
- NIH (HL106598, R01HL116571)
- NSF (CHE-1148641)
- ACS-PRF (52801-ND4)
- Grants-in Aid for Scientific Research from the Ministry of Education, Culture, Sports, Sciences, and Technology (MEXT), Japan
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Physical Sciences › Chemistry › Organic Chemistry › Sulfur-Based Synthesis Techniques
- Keywords
- hydrogen sulfide, hydropersulfides, redox chemistry
- MeSH terms
- Animals, Cell Communication, Disulfides, Humans, Hydrogen Sulfide, Oxidation-Reduction, Signal Transduction, Biosynthetic Pathways
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
