ArticleMolecular and cellular biochemistry2019
Hydrogen bond-linked pathways of peptide units and polar groups of amino acid residues suitable for electron transfer in cytochrome c proteins.
Article in Molecular and cellular biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed, 6 citations in OpenAlex.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Electron transfer occurs through heme-Fe across the cytochrome c protein. The current models of long range electron transfer pathways in proteins include covalent σ-bonds, van der Waals forces, and through space jump. Hydrogen-bond-linked pathways of delocalized electron units in peptide units and polar side chains of amino acid residues in proteins and internal water molecules are better suited for intramolecular atom-to-atom electron transfer in proteins. Crystal structures of cytochrome c proteins from horse (1HRC), tuna (3CYT), rice (1CCR), and yeast (3CX5) were analyzed using pymol software for 'Hydrogen Bonds' marking the polar atoms within the distance of 2.6-3.3 Å and tracing the atom-to-atom pathways linked by hydrogen bonds. Pathways of hydrogen-bond-linked peptide units, polar side chains of the amino acid residues, and buried water molecules connect heme-Fe through axially coordinated Met80-S and His18-N have been traced in cytochrome c proteins obtained from horse, tuna, rice and yeast with an identical hydrogen-bonded sequence around the heme-Fe: Asn-N-water-O-Tyr-O-Met-S-heme-Fe-His (HN-C=N)-Pro-Asn-Pro-Gly (peptide unit, HN-C=O)-water-O. More than half of the amino acid residues in these pathways are among the conserved list and delocalized electron units, internal water molecules and hydrogen bonds are conspicuous by their presence.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.