English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Electrostatic profiling of photosynthetic pigments: implications for directed spectral tuning

Sirohiwal, A., & Pantazis, D. A. (2021). Electrostatic profiling of photosynthetic pigments: implications for directed spectral tuning. Physical Chemistry Chemical Physics, 23(43), 24677-24684. doi:10.1039/D1CP02580E.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Sirohiwal, Abhishek1, Author              
Pantazis, Dimitrios A.1, Author              
Affiliations:
1Research Group Pantazis, Max-Planck-Institut für Kohlenforschung, Max Planck Society, ou_2541711              

Content

show
hide
Free keywords: -
 Abstract: Photosynthetic pigment–protein complexes harvest solar energy with a high quantum efficiency. Protein scaffolds are known to tune the spectral properties of embedded pigments principally through structured electrostatic environments. Although the physical nature of electrostatic tuning is straightforward, the precise spatial principles of electrostatic preorganization remain poorly explored for different protein matrices and incompletely characterized with respect to the intrinsic properties of different photosynthetic pigments. In this work, we study the electronic structure features associated with the lowest excited state of a series of eight naturally occurring (bacterio)chlorophylls and pheophytins to describe the precise topological differences in electrostatic potentials and hence determine intrinsic differences in the expected mode and impact of electrostatic tuning. The difference electrostatic potentials between the ground and first excited states are used as fingerprints. Both the spatial profile and the propensity for spectral tuning are found to be unique for each pigment, indicating spatially and directionally distinct modes of electrostatic tuning. The results define a specific partitioning of the protein matrix around each pigment as an aid to identify regions with a maximal impact on spectral tuning and have direct implications for dimensionality reduction in protein design and engineering. Thus, a quantum mechanical basis is provided for understanding, predicting, and ultimately designing sequence-modified or pigment-exchanged biological systems, as suggested for selected examples of pigment-reconstituted proteins.

Details

show
hide
Language(s): eng - English
 Dates: 2021-06-082021-10-082021-11-21
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1039/D1CP02580E
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Physical Chemistry Chemical Physics
  Abbreviation : Phys. Chem. Chem. Phys.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Cambridge, England : Royal Society of Chemistry
Pages: - Volume / Issue: 23 (43) Sequence Number: - Start / End Page: 24677 - 24684 Identifier: ISSN: 1463-9076
CoNE: https://pure.mpg.de/cone/journals/resource/954925272413_1