![Proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor | Scientific Reports Proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor | Scientific Reports](https://media.springernature.com/full/springer-static/image/art%3A10.1038%2Fsrep43880/MediaObjects/41598_2017_Article_BFsrep43880_Fig1_HTML.jpg)
Proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor | Scientific Reports
![Figure 1 from Active site probes of flavoproteins. Determination of the solvent accessibility of the flavin position 8 for a series of flavoproteins. | Semantic Scholar Figure 1 from Active site probes of flavoproteins. Determination of the solvent accessibility of the flavin position 8 for a series of flavoproteins. | Semantic Scholar](https://d3i71xaburhd42.cloudfront.net/e7502dc1572670bb45265c4e0d89e2704c13ab67/2-Figure1-1.png)
Figure 1 from Active site probes of flavoproteins. Determination of the solvent accessibility of the flavin position 8 for a series of flavoproteins. | Semantic Scholar
![Modulating catalytic activity of a modified flavin analogue via judicially positioned metal ion toward aerobic sulphoxidation - RSC Advances (RSC Publishing) DOI:10.1039/D1RA06558K Modulating catalytic activity of a modified flavin analogue via judicially positioned metal ion toward aerobic sulphoxidation - RSC Advances (RSC Publishing) DOI:10.1039/D1RA06558K](https://pubs.rsc.org/image/article/2022/RA/d1ra06558k/d1ra06558k-s1_hi-res.gif)
Modulating catalytic activity of a modified flavin analogue via judicially positioned metal ion toward aerobic sulphoxidation - RSC Advances (RSC Publishing) DOI:10.1039/D1RA06558K
![SOLVED: The reactive part of FAD is and the reactive part of NAD+ is an isoalloxazine ring; a nicotinamide ring b) niacin; an isoalloxazine ring an isoalloxazine ring; niacin nicotinamide ring; an SOLVED: The reactive part of FAD is and the reactive part of NAD+ is an isoalloxazine ring; a nicotinamide ring b) niacin; an isoalloxazine ring an isoalloxazine ring; niacin nicotinamide ring; an](https://cdn.numerade.com/ask_images/afd6390c129345dd80c8b52618ceca0f.jpg)
SOLVED: The reactive part of FAD is and the reactive part of NAD+ is an isoalloxazine ring; a nicotinamide ring b) niacin; an isoalloxazine ring an isoalloxazine ring; niacin nicotinamide ring; an
![SOLVED: (Q47) Which of the following statements is correct regarding what happens during the reduction of FAD? A flavin group is transferred An equivalent of hydride ion is transferred The isoalloxazine ring SOLVED: (Q47) Which of the following statements is correct regarding what happens during the reduction of FAD? A flavin group is transferred An equivalent of hydride ion is transferred The isoalloxazine ring](https://cdn.numerade.com/ask_images/facd738b3fd94d1aa8df632ce57f8fb7.jpg)
SOLVED: (Q47) Which of the following statements is correct regarding what happens during the reduction of FAD? A flavin group is transferred An equivalent of hydride ion is transferred The isoalloxazine ring
The ins and outs of vanillyl alcohol oxidase: Identification of ligand migration paths | PLOS Computational Biology
![Isoalloxazine Ring of FAD Is Required for the Formation of the Core in the Hsp60-assisted Folding of Medium Chain Acyl-CoA Dehydrogenase Subunit into the Assembly Competent Conformation in Mitochondria (∗) - Journal Isoalloxazine Ring of FAD Is Required for the Formation of the Core in the Hsp60-assisted Folding of Medium Chain Acyl-CoA Dehydrogenase Subunit into the Assembly Competent Conformation in Mitochondria (∗) - Journal](https://www.jbc.org/cms/asset/98c95f56-f715-439d-a807-e1418809b1f4/gr1.jpg)
Isoalloxazine Ring of FAD Is Required for the Formation of the Core in the Hsp60-assisted Folding of Medium Chain Acyl-CoA Dehydrogenase Subunit into the Assembly Competent Conformation in Mitochondria (∗) - Journal
3 Structure of isoalloxazine ring system with ribityl chain where X =-H... | Download Scientific Diagram
Electronic transitions in the isoalloxazine ring and orientation of flavins in model membranes studied by polarized light spectroscopy | Biochemistry
![Solid-State Structural Properties of Alloxazine Determined from Powder XRD Data in Conjunction with DFT-D Calculations and Solid-State NMR Spectroscopy: Unraveling the Tautomeric Identity and Pathways for Tautomeric Interconversion | Crystal Growth & Solid-State Structural Properties of Alloxazine Determined from Powder XRD Data in Conjunction with DFT-D Calculations and Solid-State NMR Spectroscopy: Unraveling the Tautomeric Identity and Pathways for Tautomeric Interconversion | Crystal Growth &](https://pubs.acs.org/cms/10.1021/acs.cgd.1c01114/asset/images/large/cg1c01114_0001.jpeg)
Solid-State Structural Properties of Alloxazine Determined from Powder XRD Data in Conjunction with DFT-D Calculations and Solid-State NMR Spectroscopy: Unraveling the Tautomeric Identity and Pathways for Tautomeric Interconversion | Crystal Growth &
![PDF) Theoretical analysis of the electron spin density distribution of the flavin semiquinone isoalloxazine ring within model protein environments | Jesus Martinez - Academia.edu PDF) Theoretical analysis of the electron spin density distribution of the flavin semiquinone isoalloxazine ring within model protein environments | Jesus Martinez - Academia.edu](https://0.academia-photos.com/attachment_thumbnails/46302231/mini_magick20190210-22705-1gl3pai.png?1549797184)
PDF) Theoretical analysis of the electron spin density distribution of the flavin semiquinone isoalloxazine ring within model protein environments | Jesus Martinez - Academia.edu
![Flavogenomics – a genomic and structural view of flavin‐dependent proteins - Macheroux - 2011 - The FEBS Journal - Wiley Online Library Flavogenomics – a genomic and structural view of flavin‐dependent proteins - Macheroux - 2011 - The FEBS Journal - Wiley Online Library](https://febs.onlinelibrary.wiley.com/cms/asset/8f590850-e1d7-4ffc-89ae-441b31d28f97/febs_8202_f1.gif)
Flavogenomics – a genomic and structural view of flavin‐dependent proteins - Macheroux - 2011 - The FEBS Journal - Wiley Online Library
![The chemical activities of bacteria. Bacteria. PROSTHETIC GROUPS 33 This forms the prosthetic group of enzymes known as flavoproteins and again acts as hydrogen carrier by alternate reduction and oxidation of The chemical activities of bacteria. Bacteria. PROSTHETIC GROUPS 33 This forms the prosthetic group of enzymes known as flavoproteins and again acts as hydrogen carrier by alternate reduction and oxidation of](https://c8.alamy.com/comp/RJ9FTN/the-chemical-activities-of-bacteria-bacteria-prosthetic-groups-33-this-forms-the-prosthetic-group-of-enzymes-known-as-flavoproteins-and-again-acts-as-hydrogen-carrier-by-alternate-reduction-and-oxidation-of-the-double-bond-in-the-isoalloxazine-ring-riboflavin-phosphate-consists-of-riboflavin-with-a-single-phosphate-radicle-occurs-as-the-prosthetic-group-of-a-flavoprotein-enzyme-known-as-cytochrome-reductase-see-below-thiamindiphosphate-aneurindiphosphate-or-cocarboxylase-n==c-nhi-ch3-0-0-i-i-ci-c==c-ch2-ch20p-o-p-oh-h3cc-c-ch2-n-i-oh-oh-ii-ii-c-1-n-ch-h-thiamindiphosphate-was-RJ9FTN.jpg)