Biosynthesis of Open‐Chain Tetrapyrroles in Plants, Algae, and Cyanobacteria

Beale, Samuel I.

doi:10.1002/9780470514535.ch9

Cited by 22 publications

(19 citation statements)

References 47 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This research completes our understanding of how the tetrapyrrole pigments of life, namely, siroheme (22), hemes (23,24), bilins (25,26), vitamin B 12 (27), coenzyme F 430 (28,29), and now Chls, are synthesized from a common template. By identifying the elusive oxidative ring cyclase step that confers the green color to Chl, we have been able to assemble a cyclase gene, together with 11 others, to form a Chl biosynthetic pathway in E. coli.…”

Section: Discussionsupporting

confidence: 58%

Complete enzyme set for chlorophyll biosynthesis in Escherichia coli

et al. 2018

View full text Add to dashboard Cite

show abstract

Section: Discussionsupporting

confidence: 58%

Complete enzyme set for chlorophyll biosynthesis in Escherichia coli

et al. 2018

View full text Add to dashboard Cite

show abstract

“…HO cleaves the α-meso carbon bridge of heme, yielding equimolar quantities of carbon monoxide (CO), iron ions and BV (Figure 1). HO seems to be ubiquitously present in photosynthetic bacteria and plants as a key enzyme for the synthesis of photon-accepting chromophores (Beale, 1994; Davis et al, 1999; Migita et al, 2003). In mammals, HO has three major isoforms of which HO1 is inducible by oxidative stress, HO2 is constitutive, and HO3 is a pseudotranscript of HO2 (Abraham and Kappas, 2008).…”

Section: Introductionmentioning

confidence: 99%

How to Increase Brightness of Near-Infrared Fluorescent Proteins in Mammalian Cells

Shemetov

Oliinyk

Verkhusha

2017

Cell Chemical Biology

View full text Add to dashboard Cite

SUMMARY Numerous near-infrared (NIR) fluorescent proteins (FPs) were recently engineered from bacterial photoreceptors but lack of their systematic comparison makes researcher’s choice rather difficult. Here we evaluated side-by-side several modern NIR FPs, such as blue-shifted smURFP and miRFP670, and red-shifted mIFP and miRFP703. We found that among all NIR FPs, miRFP670 had the highest fluorescence intensity in various mammalian cells. For instance in common HeLa cells miRFP703, mIFP and smURFP were 2-, 9- and 53-fold dimmer than miRFP670. Either co-expression of heme oxygenase or incubation of cells with heme precursor weakly affected NIR fluorescence, however, in the latter case elevated cellular autofluorescence. Exogenously added chromophore substantially increased smURFP brightness but only slightly enhanced brightness of other NIR FPs. mIFP showed intermediate while monomeric miRFP670 and miRFP703 exhibited high binding efficiency of endogenous biliverdin chromophore. This feature makes them easy to use as GFP-like proteins for spectral multiplexing with FPs of visible range.

show abstract

“…In mammals the products serve as a precursor for the potent antioxidant bilirubin, as a source of ~97% of the required iron, and as a gaseous neuronal messenger, respectively (4–7). The product biliverdin is converted to photosynthetic pigments in plants and cyanobacteria, (8) while in some pathogenic bacteria the primary function is to secure iron. (4, 6) All HOs proceed via the same three intermediates, meso-hydroxyhemin, verdoheme and iron-biliverdin (Scheme 1), and exhibit significant sequence (4, 6) and structural homology with a conserved α-helical fold (9–15).…”

mentioning

confidence: 99%

Influence of Substrate Modification and C-Terminal Truncation on the Active Site Structure of Substrate-Bound Heme Oxygenase from Neisseriae meningitidis. A ¹H NMR Study

Peng

Satterlee

et al. 2011

Biochemistry

View full text Add to dashboard Cite

Heme oxygenase, HO, from the pathogenic bacterium N. meningitidis, NmHO, which secures host iron, shares many properties with mammalian HOs, but also exhibits some key differences. The crystal structure appears more compact and the crystal-undetected C-terminus interacts with substrate in solution. The unique nature of substrate-protein, specifically pyrrole-I/II-helix-2, peripheral interactions in NmHO are probed by 2D 1H NMR to reveal unique structural features controlling substrate orientation. The thermodynamics of substrate orientational isomerism are mapped for substrates with individual vinyl → methyl → hydrogen substitutions and with enzyme C-terminal deletions. NmHO exhibits significantly stronger orientational preference, reflecting much stronger and selective pyrrole-I/II interactions with the protein matrix, than in mammalian HOs. Thus, replacing bulky vinyls with hydrogens results in a 180° rotation of substrate about the α,γ-meso axis in the active site. A "collapse" of the substrate pocket as substrate size decreases is reflected in movement of helix-2 toward the substrate as indicated by significant and selective increased NOESY cross peak intensity, increase in steric Fe-CN tilt reflected in the orientation of the major magnetic axis, and decrease in steric constraints controlling the rate of aromatic ring reorientation. The active site of NmHO appears "stressed" for native protohemin and its "collapse" upon replacing vinyls by hydrogen leads to a factor ~102 increase in substrate affinity. Interaction of the C-terminus with the active site destabilizes the crystallographic protohemin orientation by ~0.7 kcal/mol, which is consistent with optimizing the His207-Asp27 H-bond. Implications of the active site "stress" for product release are discussed.

show abstract

Biosynthesis of Open‐Chain Tetrapyrroles in Plants, Algae, and Cyanobacteria

Cited by 22 publications

References 47 publications

Complete enzyme set for chlorophyll biosynthesis in Escherichia coli

Complete enzyme set for chlorophyll biosynthesis in Escherichia coli

How to Increase Brightness of Near-Infrared Fluorescent Proteins in Mammalian Cells

Influence of Substrate Modification and C-Terminal Truncation on the Active Site Structure of Substrate-Bound Heme Oxygenase from Neisseriae meningitidis. A ¹H NMR Study

Contact Info

Product

Resources

About

Biosynthesis of Open‐Chain Tetrapyrroles in Plants, Algae, and Cyanobacteria

Cited by 22 publications

References 47 publications

Complete enzyme set for chlorophyll biosynthesis in Escherichia coli

Complete enzyme set for chlorophyll biosynthesis in Escherichia coli

How to Increase Brightness of Near-Infrared Fluorescent Proteins in Mammalian Cells

Influence of Substrate Modification and C-Terminal Truncation on the Active Site Structure of Substrate-Bound Heme Oxygenase from Neisseriae meningitidis. A 1H NMR Study

Contact Info

Product

Resources

About

Influence of Substrate Modification and C-Terminal Truncation on the Active Site Structure of Substrate-Bound Heme Oxygenase from Neisseriae meningitidis. A ¹H NMR Study