Lucina pectinata oxyhemoglobin (II-III) heterodimer pH susceptibility

Marchany-Rivera, Darya; Smith, Clyde A.; Rodriguez-Perez, Josiris D.; López-Garriga, Juan

doi:10.1016/j.jinorgbio.2020.111055

Lucina pectinata oxyhemoglobin (II-III) heterodimer pH susceptibility

Journal Article · Sat Mar 07 00:00:00 EST 2020 · Journal of Inorganic Biochemistry

DOI:https://doi.org/10.1016/j.jinorgbio.2020.111055· OSTI ID:1638048

Marchany-Rivera, Darya ^[1]; Smith, Clyde A. ^[2]; Rodriguez-Perez, Josiris D. ^[1]; López-Garriga, Juan ^[1]

Univ. of Puerto Rico, Mayaguez (Puerto Rico)
SLAC National Accelerator Lab., Menlo Park, CA (United States)

Lucina pectinata live in high concentrations of hydrogen sulfide (H₂S) and contains one hemoglobin, Hemoglobin I (HbI), transporting H₂S and two hemoglobins, Hemoglobin II (HbII) and Hemoglobin (HbIII), transferring dioxygen to symbionts. HbII and HbIII contain B10 tyrosine (Tyr) and E7 glutamine (Gln) in the heme pocket generating an efficient hydrogen bonding network with the (HbII-HbIII)-O₂ species, leading to very low ligand dissociation rates. The results indicate that the oxy-hemeprotein is susceptible to pH from 4 to 9, at acidic conditions, and as a function of the potassium ferricyanide concentration, 100% of the met-aquo derivative is produced. Without a strong oxidant, pH 5 generates a small concentration of the met-aquo complex. The process is accelerated by the presence of salts, as indicated by the crystallization structures and UV–Vis spectra. The results suggest that acidic pH generates conformational changes associated with B10 and E7 heme pocket amino acids, weakening the (HbII-HbIII)-O₂ hydrogen bond network. The observation is supported by X-ray crystallography, since at pH 4 and 5, the heme-Fe tends to oxidize, while at pH 7, the oxy-heterodimer is present. Additionally, conformational changes are observed at higher pH by the presence of a 605 nm transition associated with the iron heme-Tyr interaction. Therefore, pH is one crucial factor regulating the (HbII-HbIII)-O₂ complex hydrogen-bonding network. Thus, it can be proposed that the hydrogen bonding adjustments between the heme bound O₂ and the Tyr and Gln amino acids contribute to oxygen dissociation from the (HbII-HbIII)-O₂ system.

View Accepted Manuscript (DOE)

Research Organization:: SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)

Sponsoring Organization:: NACME; NIH; NSF; National Institute of General Medical Sciences; USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER)

Grant/Contract Number:: AC02-76SF00515

OSTI ID:: 1638048

Alternate ID(s):: OSTI ID: 1692089

Journal Information:: Journal of Inorganic Biochemistry, Journal Name: Journal of Inorganic Biochemistry Journal Issue: C Vol. 207; ISSN 0162-0134

Publisher:: ElsevierCopyright Statement

Country of Publication:: United States

Language:: English

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Hemoprotein
glutamine
oxygen release
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tyrosine

Lucina pectinata oxyhemoglobin (II-III) heterodimer pH susceptibility

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References (53)

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