Mårten Wikström

ORCID: 0000-0002-7527-4415
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About
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Research Areas
  • Photosynthetic Processes and Mechanisms
  • Photoreceptor and optogenetics research
  • Mitochondrial Function and Pathology
  • Hemoglobin structure and function
  • ATP Synthase and ATPases Research
  • Electrochemical Analysis and Applications
  • Spectroscopy and Quantum Chemical Studies
  • Oral microbiology and periodontitis research
  • Electrochemical sensors and biosensors
  • Metal-Catalyzed Oxygenation Mechanisms
  • Mass Spectrometry Techniques and Applications
  • Electron Spin Resonance Studies
  • Metabolism and Genetic Disorders
  • Porphyrin and Phthalocyanine Chemistry
  • Salivary Gland Disorders and Functions
  • Lipid Membrane Structure and Behavior
  • thermodynamics and calorimetric analyses
  • Metalloenzymes and iron-sulfur proteins
  • Light effects on plants
  • Streptococcal Infections and Treatments
  • Ion Transport and Channel Regulation
  • HIV/AIDS oral health manifestations
  • Adipose Tissue and Metabolism
  • Heme Oxygenase-1 and Carbon Monoxide
  • Protein Structure and Dynamics

University of Helsinki
2015-2024

Biocenter Finland
1998-2023

Örebro University
2020-2021

European Society of Radiology
2020

Tallaght University Hospital
2020

Region Östergötland
2018

Helsinki Institute of Physics
2009-2018

Region of Southern Denmark
2018

Czech Academy of Sciences, Institute of Biotechnology
1995-2015

California Institute of Technology
2007-2012

10.1016/0005-2728(72)90258-7 article EN Biochimica et Biophysica Acta (BBA) - Bioenergetics 1972-12-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTProperties of the two terminal oxidases Escherichia coliAnne Puustinen, Moshe Finel, Tuomas Haltia, Robert B. Gennis, and Marten WikstromCite this: Biochemistry 1991, 30, 16, 3936–3942Publication Date (Print):April 23, 1991Publication History Published online1 May 2002Published inissue 23 April 1991https://pubs.acs.org/doi/10.1021/bi00230a019https://doi.org/10.1021/bi00230a019research-articleACS PublicationsRequest reuse permissionsArticle...

10.1021/bi00230a019 article EN Biochemistry 1991-04-23

10.1016/s0005-2728(03)00041-0 article EN Biochimica et Biophysica Acta (BBA) - Bioenergetics 2003-05-19

The spectrophotometric indicators neutral red and safranine were used to determine the relative H + /e − ratios of proton uptake from mitochondrial matrix, q electrical charge translocation, during oxidation β‐OH‐butyrate succinate by ferricyanide in rat liver mitochondria. With both higher than with a factor close 3.0. Since there is full agreement that translocation are equal unity for (or ubiquinol) ferricytochrome c , corresponding NADH ubiquinone cytochrome near 2.0 3.0, respectively.

10.1016/0014-5793(84)80338-5 article EN FEBS Letters 1984-04-24

Porphyromonas gingivalis, a Gram-negative anaerobic rod, has been closely associated with the initiation and progression of periodontal disease. This organism shown to produce large number proteolytic enzymes which can degrade variety tissue proteins, these are considered be major virulence factors. One proteinases produced by this organism, referred as gingipain-1, purified homogeneity from P. gingivalis culture medium combination gel filtration ion-exchange chromatography. The enzyme was...

10.1016/s0021-9258(19)37045-0 article EN cc-by Journal of Biological Chemistry 1992-09-01

Spheroplasts from aerobically grown wild‐type Paracoccus denitrificans cells respire with succinate despite specific inhibition of the cytochrome bc 1 complex by myxothiazol. Coupled to this activity, which involves only b ‐type cytochromes, there is translocation 1.5–1.9 H + /e − across cytoplasmic membrane. Similar ratios are observed during oxidation ubiquinol in spheroplasts mutants lacking c oxidase, or deficient , as well a strain E. coli d was deleted. These observations show that o...

10.1016/0014-5793(89)80616-7 article EN FEBS Letters 1989-06-05

Cytochrome c oxidase catalyzes most of the biological oxygen consumption on Earth, a process responsible for energy supply in aerobic organisms. This remarkable membrane-bound enzyme also converts free from O(2) reduction to an electrochemical proton gradient by functioning as redox-linked pump. Although structures several oxidases are known, molecular mechanism translocation has remained elusive. Here, correlated internal electron and transfer reactions were tracked real time spectroscopic...

10.1073/pnas.0608794104 article EN Proceedings of the National Academy of Sciences 2007-02-10

Diphenyleneiodonium (DPI) inhibits the mitochondrial NADH-ubiquinone oxidoreductase (Complex I) on substrate side of Fe-S clusters.In inhibited NADH-supplemented state all clusters are oxidized, whereas reduced minus oxidized difference spectrum protein-bound FMN can be visualized.It is characterized by troughs at 370 and 450 nm a small increase absorbance in 500-700-nm region.DPI probably reacts irreversibly with FMN, because oxidation blocked even after its extraction from...

10.1016/s0021-9258(17)31926-9 article EN cc-by Journal of Biological Chemistry 1994-08-01
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