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Photochemistry Governing Bacteriorhodopsin and Bacterial Reaction Center

Author

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  • Bernadine G Ang
  • Friedrich Schotte

    (University of the Philippines Diliman, Philippines)

Abstract

Bacteriorhodopsin (bR) is a light driven proton pump that converts sunlight to chemical energy. BR is an integral membrane structured protein found in the purple membrane of Halobacterium halobium. It is composed of 248 amino acids and a chromophore in the middle which captures light. Electricity can be generated through the process of light-chemical conversion, when photons are absorbed by thechromophore, the photo cycle begins. Bacterial Reaction Center (bRC) is a light driven electron transfer reaction that converts solar energy to chemical energy. bRC are integral membrane structured proteins found in the purple membrane of Rhodobacter sphaeroides. It is composed of 3 major co-factors such as bacteriochlorophylls, bacteriopheophytin and quinone. Its primary mechanism is to execute photo synthesis. In this interaction, electron transfer occurs through light ejection of electron that passes through the membrane. Conversion of sunlight to chemical energy simultaneously precipitates. This review aims to compare the function and structure of Bacteriorhodopsin and bacterial reaction centers, underscoring the energy generated in both membranes. Through calculating the ATP, protons and photons that cross the membrane, exact value of energy emission in the order of electron volts present the energy generated. Advantages and mechanisms of photoreactions including bioelectronic, bio energy production in bacteriorhodopsin and bacterial reaction centers will be exemplified. Ultimately, energy efficiency of bacteriorhodopsin and bacterial reaction center will be determined.

Suggested Citation

  • Bernadine G Ang & Friedrich Schotte, 2018. "Photochemistry Governing Bacteriorhodopsin and Bacterial Reaction Center," JOJ Sciences, Juniper Publishers Inc., vol. 1(2), pages 31-33, May.
    • Handle: RePEc:adp:oajojs:v:1:y:2018:i:2:p:31-33
    DOI: 10.19080/JOJS.2018.01.555559
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