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Electron Transfer in Photosynthesis

A special issue of Applied Sciences (ISSN 2076-3417). This special issue belongs to the section "Chemical and Molecular Sciences".

Deadline for manuscript submissions: closed (22 April 2022) | Viewed by 2691

Special Issue Editor


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Guest Editor
Instituto de Bioquímica Vegetal y Fotosíntesis, Centro de Investigaciones Científicas Isla de la Cartuja, Universidad de Sevilla y CSIC, Américo Vespucio 49, E-41092 Sevilla, Spain
Interests: study of the structure-function relationship of metalloproteins that intervene in electron transfer reactions in the photosynthetic and respiratory electron transfer chains and in detoxification of reactive oxygen species, development of new biofertilizers with a high capacity for N2 fixation, and biofuels production

Special Issue Information

Dear Colleagues,

A crucial process in living photoautotrophic organisms is the acquisition, conversion, and conservation of solar energy, which occurs through photosynthesis. Plants, algae, and some bacteria utilize energy from sunlight and convert and store it into chemical compounds. This energy can be metabolized by said organisms or by others, facilitating anabolic processes, the transport of substances through membranes, or the movement of the organism itself. Energy conversion occurs in so-called electron transport chains, in which energy is converted into a proton gradient and into reducing power. This conversion is carried out by oxidation-reduction reactions in which electrons are transferred along a series of protein complexes integrated in membranes and connected to each other by soluble transporters.

This Special Issue is intended for the publication of both original works and reviews in the field of the electron transfer processes that occur during photosynthesis. Studies of photosynthesis mechanisms are of current interest. Knowledge of the photosynthetic electron transfer process and related pathways can contribute to the development of the field of bioenergetics in order to address issues which are crucial to everyday human life. The purpose of this Special Issue is to offer a broad overview of the state of the art in the field of electron transfer reactions that occur in the photosynthetic electron transfer chain through an interdisciplinary approach, ranging from biochemistry to chemistry, including technology, biofuel production, and industrial applications.

Dr. Fernando P. Molina-Heredia
Guest Editor

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Keywords

  • Antenna complex
  • Bioenergy
  • Biofuel
  • Cyclic electron flow
  • Cyclic photophosphorylation
  • Cytochrome b6-f complex
  • Cytochrome c6
  • Electron transport
  • Ferredoxin
  • Phycobilisome
  • Flavodoxin
  • Light-harvesting system
  • Light-dependent reactions
  • Light stress
  • Linear electron flow
  • Non-cyclic photophosphorylation
  • Non-photochemical quenching
  • Photoinhibition
  • Photolysis
  • Photosystem I
  • Photosystem II
  • Plastocyanin
  • Plastoquinone
  • Reactive oxygen species
  • Regulation
  • Renewable energy

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Published Papers (1 paper)

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Research

8 pages, 4124 KiB  
Communication
Cytochrome cM Is Probably a Membrane Protein Similar to the C Subunit of the Bacterial Nitric Oxide Reductase
by Tomás Rodríguez-Gil, Alejandro Torrado, Macarena Iniesta-Pallarés, Consolación Álvarez, Vicente Mariscal and Fernando P. Molina-Heredia
Appl. Sci. 2021, 11(20), 9396; https://doi.org/10.3390/app11209396 - 10 Oct 2021
Cited by 3 | Viewed by 2176
Abstract
Cytochrome cM was first described in 1994 and its sequence has been found in the genome of manifold cyanobacterial species ever since. Numerous studies have been carried out with the purpose of determining its function, but none of them has given place [...] Read more.
Cytochrome cM was first described in 1994 and its sequence has been found in the genome of manifold cyanobacterial species ever since. Numerous studies have been carried out with the purpose of determining its function, but none of them has given place to conclusive results so far. Many of these studies are based on the assumption that cytochrome cM is a soluble protein located in the thylakoid lumen of cyanobacteria. In this work, we have reevaluated the sequence of cytochrome cM, with our results showing that its most probable 3D structure is strongly similar to that of the C subunit of the bacterial nitric oxide reductase. The potential presence of an α-helix tail, which could locate this protein in the thylakoid membrane, further supports this hypothesis, thus providing a new, unexpected role for this redox protein. Full article
(This article belongs to the Special Issue Electron Transfer in Photosynthesis)
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