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Analysis of institutional authors

Martínez-Costa óhAuthorSamhan-Arias AkCorresponding Author
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Structural features of cytochrome b5 –cytochrome b5 reductase complex formation and implications for the intramolecular dynamics of cytochrome b5 reductase

Publicated to:INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES. 23 (1): 118- - 2022-01-01 23(1), DOI: 10.3390/ijms23010118

Authors: Gutiérrez-Merino C; Martínez-Costa OH; Monsalve M; Samhan-Arias AK

Affiliations

CSIC-UAM - Instituto de Investigaciones Biomédicas Alberto Sols (IIBM) - Author
Inst Invest Biomed Alberto Sols CSIC UAM, Arturo Duperier,4, Madrid 28029, Spain - Author
Univ Autonoma Madrid UAM, Dept Biochem, Fac Med, Arzobispo Morcillo,4, Madrid 28029, Spain - Author
Univ Extremadura, Dept Biochem & Mol Biol, Fac Sci, Av Elvas S-N, Badajoz 06006, Spain - Author
Univ Extremadura, Inst Biomarcadores Patol Mol, Av Elvas S-N, Badajoz 06006, Spain - Author
Universidad Autónoma de Madrid , CSIC-UAM - Instituto de Investigaciones Biomédicas Alberto Sols (IIBM) - Author
Universidad de Extremadura - Author
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Abstract

Membrane cytochrome b5 reductase is a pleiotropic oxidoreductase that uses primarily soluble reduced nicotinamide adenine dinucleotide (NADH) as an electron donor to reduce mul-tiple biological acceptors localized in cellular membranes. Some of the biological acceptors of the reductase and coupled redox proteins might eventually transfer electrons to oxygen to form reactive oxygen species. Additionally, an inefficient electron transfer to redox acceptors can lead to electron uncoupling and superoxide anion formation by the reductase. Many efforts have been made to characterize the involved catalytic domains in the electron transfer from the reduced flavoprotein to its electron acceptors, such as cytochrome b5, through a detailed description of the flavin and NADH-binding sites. This information might help to understand better the processes and modifi-cations involved in reactive oxygen formation by the cytochrome b5 reductase. Nevertheless, more than half a century since this enzyme was first purified, the one-electron transfer process toward potential electron acceptors of the reductase is still only partially understood. New advances in computational analysis of protein structures allow predicting the intramolecular protein dynamics, identifying potential functional sites, or evaluating the effects of microenvironment changes in protein structure and dynamics. We applied this approach to characterize further the roles of amino acid domains within cytochrome b5 reductase structure, part of the catalytic domain, and several sensors and structural domains involved in the interactions with cytochrome b5 and other electron acceptors. The computational analysis results allowed us to rationalize some of the available spectroscopic data regarding ligand-induced conformational changes leading to an increase in the flavin adenine dinucleotide (FAD) solvent-exposed surface, which has been previously correlated with the formation of complexes with electron acceptors.

Keywords
ascorbatecytochrome b(5)cytochrome b5cytochrome b5 reductaseelectron transferelectron-transfermutationsmyristic acidnadh-cytochrome-b(5) reductaseouter mitochondrialplasma-membraneprotein intrinsic dynamicssequencesuperoxide anion radicalvitamin-eCytochrome b reductase 5Cytochrome b 5Cytochrome b(5) reductaseElectron transferProtein intrinsic dynamicsSuperoxide anion radicalSuperoxide-anion

Quality index

Bibliometric impact. Analysis of the contribution and dissemination channel

The work has been published in the journal INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES due to its progression and the good impact it has achieved in recent years, according to the agency WoS (JCR), it has become a reference in its field. In the year of publication of the work, 2022, it was in position 66/285, thus managing to position itself as a Q1 (Primer Cuartil), in the category Biochemistry & Molecular Biology.

From a relative perspective, and based on the normalized impact indicator calculated from World Citations provided by WoS (ESI, Clarivate), it yields a value for the citation normalization relative to the expected citation rate of: 1.05. This indicates that, compared to works in the same discipline and in the same year of publication, it ranks as a work cited above average. (source consulted: ESI Nov 14, 2024)

This information is reinforced by other indicators of the same type, which, although dynamic over time and dependent on the set of average global citations at the time of their calculation, consistently position the work at some point among the top 50% most cited in its field:

  • Weighted Average of Normalized Impact by the Scopus agency: 1.38 (source consulted: FECYT Feb 2024)
  • Field Citation Ratio (FCR) from Dimensions: 1.42 (source consulted: Dimensions May 2025)

Specifically, and according to different indexing agencies, this work has accumulated citations as of 2025-05-07, the following number of citations:

  • WoS: 5
  • Scopus: 8
  • Europe PMC: 5
  • OpenCitations: 8
Impact and social visibility

From the perspective of influence or social adoption, and based on metrics associated with mentions and interactions provided by agencies specializing in calculating the so-called "Alternative or Social Metrics," we can highlight as of 2025-05-07:

  • The use, from an academic perspective evidenced by the Altmetric agency indicator referring to aggregations made by the personal bibliographic manager Mendeley, gives us a total of: 7.
  • The use of this contribution in bookmarks, code forks, additions to favorite lists for recurrent reading, as well as general views, indicates that someone is using the publication as a basis for their current work. This may be a notable indicator of future more formal and academic citations. This claim is supported by the result of the "Capture" indicator, which yields a total of: 7 (PlumX).

With a more dissemination-oriented intent and targeting more general audiences, we can observe other more global scores such as:

  • The Total Score from Altmetric: 3.

It is essential to present evidence supporting full alignment with institutional principles and guidelines on Open Science and the Conservation and Dissemination of Intellectual Heritage. A clear example of this is:

  • The work has been submitted to a journal whose editorial policy allows open Open Access publication.
Leadership analysis of institutional authors

There is a significant leadership presence as some of the institution’s authors appear as the first or last signer, detailed as follows: Last Author (SAMHAN ARIAS, ALEJANDRO KHALIL).

the author responsible for correspondence tasks has been SAMHAN ARIAS, ALEJANDRO KHALIL.