Molecular oxygen migration through the xenon docking sites of human hemoglobin in the R-state.

Autor: Lepeshkevich SV; B.I. Stepanov Institute of Physics, National Academy of Sciences of Belarus, 68 Nezavisimosti Ave, Minsk 220072, Belarus. Electronic address: lepeshkevich@imaph.bas-net.by., Gilevich SN; Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus, 5 Academician V.F. Kuprevich Street, Minsk 220141, Belarus. Electronic address: gilevich@iboch.bas-net.by., Parkhats MV; B.I. Stepanov Institute of Physics, National Academy of Sciences of Belarus, 68 Nezavisimosti Ave, Minsk 220072, Belarus. Electronic address: marina@imaph.bas-net.by., Dzhagarov BM; B.I. Stepanov Institute of Physics, National Academy of Sciences of Belarus, 68 Nezavisimosti Ave, Minsk 220072, Belarus. Electronic address: bmd@imaph.bas-net.by.

Publikováno v: Biochimica et biophysica acta [Biochim Biophys Acta] 2016 Sep; Vol. 1864 (9), pp. 1110-1121. Date of Electronic Publication: 2016 Jun 07.

A study of the toxicity of two isomeric sodium hydroxymercuribenzoates.

Autor: HALEY TJ, EDWARDS LD

Publikováno v: Journal of the American Pharmaceutical Association. American Pharmaceutical Association [J Am Pharm Assoc Am Pharm Assoc] 1947 Jan; Vol. 36 (1), pp. 30-2.

Proton magnetic resonance study of p-mercuribenzoate binding and structural changes in methemoglobin.

Autor: Neya S, Morishima I

Publikováno v: Biochemistry [Biochemistry] 1980 Jan 22; Vol. 19 (2), pp. 258-65.

Homoserine dehydrogenase: spontaneous reactivation by dissociation of p-mercuribenzoate from an inactive enzyme--p-mercuribenzoate complex.

Autor: Epstein CC, Datta P

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 1977 Nov; Vol. 74 (11), pp. 4862-6.

Conformational changes in the hemoglobin S system as seen by proton binding.

Autor: Scholberg HP, Fronticelli C, Bucci E

Publikováno v: The Journal of biological chemistry [J Biol Chem] 1980 Sep 25; Vol. 255 (18), pp. 8592-8.