AMBIENTUM BIOETHICA BIOLOGIA CHEMIA DIGITALIA DRAMATICA EDUCATIO ARTIS GYMNAST. ENGINEERING EPHEMERIDES EUROPAEA GEOGRAPHIA GEOLOGIA HISTORIA HISTORIA ARTIUM INFORMATICA IURISPRUDENTIA MATHEMATICA MUSICA NEGOTIA OECONOMICA PHILOLOGIA PHILOSOPHIA PHYSICA POLITICA PSYCHOLOGIA-PAEDAGOGIA SOCIOLOGIA THEOLOGIA CATHOLICA THEOLOGIA CATHOLICA LATIN THEOLOGIA GR.-CATH. VARAD THEOLOGIA ORTHODOXA THEOLOGIA REF. TRANSYLVAN
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Authors: FRANCISCO CARRASCOZA, ADRIAN M.V. BRÂNZANIC, RADU SILAGHI-DUMITRESCU.
DOI: 10.24193/subbchem.2021.4.29
Published Online: 2021-12-30
Published Print: 2021-12-30
pp. 397-404
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The non-heme diiron protein hemerythrin (Hr) has been considered as a possible alternative for semi-artificial oxygen carriers (blood substitutes). Studies on the stability of its octameric structure have been attempted by attaching spin labels to analyze its electron paramagnetic spectroscopy (ESR) signals. Reported here are molecular dynamics results of Hr bound with 1-oxyl-2,2,5,5-tetramethylpyrroline-3methyl (MTSSL) at the Cys51 position. Our results show that the Hr-MTSSL complex is less stable than its native form. These findings help to explain ESR signals obtained experimentally. Also, these results are crucial to understand the limitations of PEGylated spin labels for protein structural analysis and suggest the need or further exploration of other alternatives.
Keywords: hemerythrin, molecular dynamics, spin label, blood substitute, diiron
