By looking at a plant externally can you tell whether a plant is C3 or C4?

Usually plants growing in dry conditions use C 4 pathways. It cannot be said
conclusively if the plant is a C3 or C4 buy looking at external appearance, some guess
can be made by looking at fleshy leaf structure.

 By looking at which internal structure of a plant can you tell whether a plant is C3 or C4?

The particularly large cells around the vascular bundles of the C4 pathway
plants are called bundle sheath cells, and the leaves which have such anatomy are
said to have ‘Kranz’ anatomy. ‘Kranz’ means ‘wreath’ and is a reflection of the
arrangement of cells. The bundle sheath cells may form several layers around the
vascular bundles; they are characterised by having a large number of chloroplasts,
thick walls impervious to gaseous exchange and no intercellular spaces.

 Even though a very few cells in a C4 plant carry out the biosynthetic –Calvin pathway, yet they are highly productive. Did you know why?

 C4 plants chemically fix carbon dioxide in the cells of the mesophyll by
adding it to the three-carbon molecule phosphoenolpyruvate (PEP), a reaction
catalyzed by an enzyme called PEP carboxylase and which creates the four-carbon
organic acid, oxaloacetic acid. Oxaloacetic acid or malate synthesized by this process
is then translocated to specialized bundle sheath cells where the enzyme, rubisco,
and other Calvin cyle enzymes are located, and where CO2 released by
decarboxylation of the four-carbon acids is then fixed by rubisco activity to the
three-carbon sugar 3-Phosphoglyceric acids.
The physical separation of rubisco from the oxygen-generating light reactions
reduces photorespiration and increases CO2 fixation and thus photosynthetic capacity
of the leaf.
C4 plants can produce more sugar than C3 plants in conditions of high light and
temperature. Many important crop plants are C4 plants including maize, sorghum,
sugarcane, and millet.

 RuBisCO is an enzyme that acts both as a carboxylase and oxygenase. You know why  RuBisCO carries out more carboxylation in C4 plants?
RuBisCO has a much greater affinity for CO2 than for O2. It is the relative concentration of O2 and CO2 that determines which of the two will bind to the enzyme. In C3 plants some O2 does bind to RuBisCO, and hence CO2 fixation is decreased.
Here the RuBP instead of being converted to 2 molecules of PGA binds with O2 to
form one molecule and phosphoglycolate in a pathway called photorespiration. In the
photorespiratory pathway, there is neither synthesis of sugars, nor of ATP. Rather it
results in the release of CO2 with the utilisation of ATP. In the photorespiratory
pathway there is no synthesis of ATP or NADPH. Therefore, photorespiration is a
wasteful process.
In C4 plants photorespiration does not occur. This is because they have a mechanism
that increases the concentration of CO2 at the enzyme site. This takes place when
the C4 acid from the mesophyll is broken down in the bundle cells to release CO2 –
this results in increasing the intracellular concentration of CO2. In turn, this ensures
that the RuBisCO functions as a carboxylase minimising the oxygenase activity.

 Suppose there were plants that had a high concentration of Chlorophyll b,
but lacked chlorophyll a, would it carry out photosynthesis? Then why do
plants have chlorophyll b and other accessory pigments?

 Though chlorophyll is the major pigment responsible for trapping light,
other thylakoid pigments like chlorophyll b, xanthophylls and carotenoids, which are
called accessory pigments, also absorb light and transfer the energy to chlorophyll a.
Indeed, they not only enable a wider range of wavelength of incoming light to be
utilized for photosyntesis but also protect chlorophyll a from photo-oxidation.
Reaction center chlorophyll-protein complexes are capable of directly absorbing light
and performing charge separation events without other chlorophyll pigments, but the
absorption cross section (the likelihood of absorbing a photon under a given light
intensity) is small. Thus, the remaining chlorophylls in the photosystem and antenna
pigment protein complexes associated with the photosystems all cooperatively
absorb and funnel light energy to the reaction center. Besides chlorophyll a, there
are other pigments, called accessory pigments, which occur in these pigment-protein
antenna complexes.


11 comments on “Photosynthesis

  1. Hey! This post couldn’t be written any better! Reading this post reminds me of my good old room mate! He always kept chatting about this. I will forward this write-up to him. Pretty sure he will have a good read. Many thanks for sharing!

  2. Finding a good supplement is one of the key factors to living a vibrant life. For me, this vitamin has always proven to be the most effective. It just gives your body what it needs and it doesn’t have all of those terrible side effects as all of the bad ones. It’s also one of the cheapest ones out there.

  3. Howdy! Someone in my Facebook group shared this website with us so I came to look it over. I’m definitely loving the information. I’m bookmarking and will be tweeting this to my followers! Wonderful blog and great style and design.

  4. I’m not sure why but this site is loading incredibly slow for me. Is anyone else having this problem or is it a issue on my end? I’ll check back later on and see if the problem still exists.

  5. After reading your blog post I browsed your website a bit and noticed you aren’t ranking nearly as well in Google as you could be. I possess a handful of blogs myself and I think you should take a look here: You’ll find it’s a very nice tool that can bring you a lot more visitors. Keep up the quality posts

post your comments here....

Fill in your details below or click an icon to log in: Logo

You are commenting using your account. Log Out /  Change )

Google photo

You are commenting using your Google account. Log Out /  Change )

Twitter picture

You are commenting using your Twitter account. Log Out /  Change )

Facebook photo

You are commenting using your Facebook account. Log Out /  Change )

Connecting to %s