ArticlePloS one2013
CO rebinding kinetics and molecular dynamics simulations highlight dynamic regulation of internal cavities in human cytoglobin.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 35 citations in OpenAlex.
- Kinetic and dynamical properties of truncated hemoglobins of the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125.Protein science : a publication of the Protein Society · 2024Article
- NO and Heme Proteins: Cross-Talk between Heme and Cysteine Residues.Antioxidants (Basel, Switzerland) · 2023Review
- Regulation of nitrite reductase and lipid binding properties of cytoglobin by surface and distal histidine mutations.Nitric oxide : biology and chemistry · 2022Article
- Unusually FastInternational journal of molecular sciences · 2021Article
- Cytoglobin deficiency potentiates Crb1-mediated retinal degeneration in rd8 mice.Developmental biology · 2020Article
- Structural and functional properties of Antarctic fish cytoglobins-1: Cold-reactivity in multi-ligand reactions.Computational and structural biotechnology journal · 2020Article
- The Greenland shark Somniosus microcephalus-Hemoglobins and ligand-binding properties.PloS one · 2017Article
- Dynamic features of carboxy cytoglobin distal mutants investigated by molecular dynamics simulations.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
- Dynamics of the heme-binding bacterial gas-sensing dissimilative nitrate respiration regulator (DNR) and activation barriers for ligand binding and escape.The Journal of biological chemistry · 2014Article
- The globin superfamily: functions in nitric oxide formation and decay.Biological chemistry · 2014Review
- Effects of distal mutation on the dynamic properties of carboxycytoglobin: a molecular dynamics simulation study.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
- Allostery in the nitric oxide dioxygenase mechanism of flavohemoglobin.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
14 authors at 6 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cytoglobin (Cygb) was recently discovered in the human genome and localized in different tissues. It was suggested to play tissue-specific protective roles, spanning from scavenging of reactive oxygen species in neurons to supplying oxygen to enzymes in fibroblasts. To shed light on the functioning of such versatile machinery, we have studied the processes supporting transport of gaseous heme ligands in Cygb. Carbon monoxide rebinding shows a complex kinetic pattern with several distinct reaction intermediates, reflecting rebinding from temporary docking sites, second order recombination, and formation (and dissociation) of a bis-histidyl heme hexacoordinated reaction intermediate. Ligand exit to the solvent occurs through distinct pathways, some of which exploit temporary docking sites. The remarkable change in energetic barriers, linked to heme bis-histidyl hexacoordination by HisE7, may be responsible for active regulation of the flux of reactants and products to and from the reaction site on the distal side of the heme. A substantial change in both protein dynamics and inner cavities is observed upon transition from the CO-liganded to the pentacoordinated and bis-histidyl hexacoordinated species, which could be exploited as a signalling state. These findings are consistent with the expected versatility of the molecular activity of this protein.
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